[ { "id": "authors:0s3fv-nkc66", "collection": "authors", "collection_id": "0s3fv-nkc66", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc57", "type": "article", "title": "Factors affecting protein synthesis in vitro in rabbit reticulocytes", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Fischer", "given_name": "Edmond H.", "clpid": "Fischer-E-H" }, { "family_name": "Keighley", "given_name": "Geoffrey", "clpid": "Keighley-G" } ], "abstract": "Rabbit reticulocytes in vitro rapidly incorporate labeled amino acids into their proteins. The process is accelerated by the plasma of every mammal investigated and also by extracts of normal erythrocytes, rabbit reticulocytes, liver, spleen, and yeast (1). We have described two sets of stimulating factors: one of these sets consists of certain amino acids (1), the other of fructose-amino acids in liver (2-4). The latter set is ineffective without the addition of iron to the reaction medium. The effect of iron has been referred to in preceding publications (2-5), but without detail. After the necessity of adding iron was recognized, in order to obtain a maximal rate of protein synthesis the reaction mixture was improved further by adding to it certain substances which depend upon added iron for their effect. These increased the effect of plasma. Eventually the total (potential as well as actual) accelerating effects of plasma and liver extract were accounted for by known substances. This led to the devising of a reaction mixture formula in which the amino acid incorporation is about five times as fast as that observed when the cells are incubated in saline.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1957-12", "series_number": "2", "volume": "229", "issue": "2", "pages": "1059-1070" }, { "id": "authors:7f68y-a4a68", "collection": "authors", "collection_id": "7f68y-a4a68", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:20131211-111009191", "type": "article", "title": "Hemoglobin Synthesis in Rabbit Reticulocytes In vitro", "author": [ { "family_name": "Kruh", "given_name": "Jacques", "clpid": "Kruh-J" }, { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" } ], "abstract": "We have reported the rapid incorporation of labeled amino acids into\nthe proteins of rabbit reticulocytes in vitro and the stimulation of this process\nby certain amino acids, iron, fructose-amino acids, glucose, and some,\nas yet, unidentified material in the filtrate of boiled plasma. The incorporation\nwas measured in the mixture of the total proteins of the reticulocytes\n(1, 2).\n\nIn the study reported here two protein fractions were isolated, the hemoglobin,\nwhich comprises more than 75 per cent of the total, and the water-insoluble\nproteins. The hemoglobin was fractionated into heme and globin.\nExperiments were carried out with four C^(14)-labeled amino acids and with\ndifferent stimulators to ascertain whether heme synthesis and amino acid\nincorporation went parallel or not.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1956-06-01", "series_number": "2", "volume": "220", "issue": "2", "pages": "905-915" }, { "id": "authors:nehme-q9j12", "collection": "authors", "collection_id": "nehme-q9j12", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc55", "type": "article", "title": "Fructose-amino acids in liver: stimuli of amino acid incorporation in vitro", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Abrams", "given_name": "Adolph", "clpid": "Abrams-A" }, { "family_name": "Lowy", "given_name": "Peter H.", "clpid": "Lowy-P-H" } ], "abstract": "We report here the method which we have used to isolate fructose-amino acids from liver, some of the characteristic chemical and physical properties of these substances, and their stimulation of amino acid incorporation in vitro into the proteins of rabbit reticulocytes.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1955-07-01", "series_number": "1", "volume": "215", "issue": "1", "pages": "111-124" }, { "id": "authors:any5d-hb666", "collection": "authors", "collection_id": "any5d-hb666", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:ABRjbc52", "type": "article", "title": "The conversion of L-histidine to glutamic acid by liver enzymes", "author": [ { "family_name": "Abrams", "given_name": "Adolph", "clpid": "Abrams-A" }, { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" } ], "abstract": "Edlbacher and Neber (1) showed in 1934 that the liver enzyme named histidase degrades histidine to NH3, formic acid, and an unknown product which on further treatment with strong alkali yields glutamic acid. This led to the suggestion that glutamic acid is a metabolic product of histidine, a suggestion that was supported by the finding that glycogen was formed from histidine about as well as from glutamic acid (2). These findings did not prove that glutamic acid was one of the products of histidine metabolism, and the idea became questionable when the evidence from subsequent investigations with non-isotopic histidine (3), imidazole-N16-histidine (4), and carboxyl-C14-histidine (5) were negative or inconclusive. \n\nIn studies on the fate of carboxyl-C14-L-histidine in the liver of rabbits after injection and after incubation with guinea pig liver slices, we have found direct evidence that glutamic acid is a major product of histdine metabolism. Another highly radioactive compound was isolated by ion exchange chromatography, whose properties with respect to chromatography and lability to alkali and acid appear to correspond to those reported for isoglutamine. Takeuchi (6) isolated and identified isoglutamine as a product of the action of urocanicase on urocanic acid, which was obtained by the action of another liver enzyme on histidine. The formation of isoglutamine as an intermediate is consistent with our finding that the label in the radioactive glutamic acid formed from carboxyl-C14-histidine is not in the \u03b1-carboxyl group, and the inference is very strong that the label is in the \u03b3-carboxyl group.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1952-09-01", "series_number": "1", "volume": "198", "issue": "1", "pages": "205-214" }, { "id": "authors:asznh-32523", "collection": "authors", "collection_id": "asznh-32523", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc52", "type": "article", "title": "Incorporation in vitro of labeled amino acids into proteins of rabbit reticuloytes", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Deasy", "given_name": "Clara L.", "clpid": "Deasy-C-L" }, { "family_name": "Haagen-Smit", "given_name": "A. J.", "clpid": "Haagen-Smit-A-J" }, { "family_name": "Keighley", "given_name": "Geoffrey", "clpid": "Keighley-G" }, { "family_name": "Lowy", "given_name": "Peter H.", "clpid": "Lowy-P-H" } ], "abstract": "Continuing our work on the incorporation of labeled amino acids into proteins (1), we have begun a study of the incorporation in vitro of C14-labeled glycine, L-histidine, L-leucine, and L-lysine into the proteins of rabbit reticulocytes. In preliminary experiments the incorporation into the hemoglobin isolated from the reticulocytes was determined. But, after it was found that plasma contains factors accelerating amino acid incorporation, it was decided to proceed as rapidly as possible toward the identification of these factors; we have, therefore, measured incorporation into the total proteins of the reticulocytes, since isolation of the hemoglobin was time-consuming. The results obtained with hemoglobin and with the total proteins are essentially the same, indicating that the other proteins of the reticulocytes incorporate amino acids at approximately the same rate as hemoglobin.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1952-06-01", "series_number": "2", "volume": "196", "issue": "2", "pages": "669-694" }, { "id": "authors:k4zst-x6y82", "collection": "authors", "collection_id": "k4zst-x6y82", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:20130515-105752738", "type": "article", "title": "The Metabolism of Proteins and Amino Acids", "author": [ { "family_name": "Borsook", "given_name": "H.", "clpid": "Borsook-H" }, { "family_name": "Dubnoff", "given_name": "J. W.", "clpid": "Dubnoff-J-W" } ], "abstract": "This year is an appropriate one for reviewing the evidence which\ninvalidated the classical theory of protein metabolism (in animals)\nepitomized in the terms \"endogenous\" and \"exogenous\" metabolism;\nthe evidence which has established the theory proposed by Borsook\n& Keighley (1) and confirmed and extended by Schoenheimer and\nhis colleagues (2) and by Tarver & Schmidt (3) will also be reviewed\nin this context.", "doi": "10.1146/annurev.bi.20.070151.001233", "issn": "0066-4154", "publisher": "Annual Reviews", "publication": "Annual Review of Biochemistry", "publication_date": "1951-07", "volume": "20", "pages": "209-226" }, { "id": "authors:vnwhr-dd788", "collection": "authors", "collection_id": "vnwhr-dd788", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc50d", "type": "article", "title": "Metabolism of C14-labeled glycine, L-histidine, L-leucine, and L-lysine", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Deasy", "given_name": "Clara L.", "clpid": "Deasy-C-L" }, { "family_name": "Haagen-Smit", "given_name": "A. J.", "clpid": "Haagen-Smit-A-J" }, { "family_name": "Keighley", "given_name": "Geoffrey", "clpid": "Keighley-G" }, { "family_name": "Lowy", "given_name": "Peter H.", "clpid": "Lowy-P-H" } ], "abstract": "A study of the rates of incorporation in vivo of labeled amino acids into tissue proteins was undertaken to find the best time at which intermediates in the process might be found. The rates observed were so fast that we decided to investigate the process in some detail. The amino acids were L-\u03b1-aminoadipic-6-C14 acid, glycine-1-C14, L-histidine-2-C14-imidazole, L-leucine-1-C14, and L-lysine-1-C14.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1950-12", "series_number": "2", "volume": "187", "issue": "2", "pages": "839-848" }, { "id": "authors:3hbkx-yzv35", "collection": "authors", "collection_id": "3hbkx-yzv35", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc50c", "type": "article", "title": "Incorporation in vitro of labeled amino acids into bone marrow cell proteins", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Deasy", "given_name": "Clara L.", "clpid": "Deasy-C-L" }, { "family_name": "Haagen-Smit", "given_name": "A. J.", "clpid": "Haagen-Smit-A-J" }, { "family_name": "Keighley", "given_name": "Geoffrey", "clpid": "Keighley-G" }, { "family_name": "Lowy", "given_name": "Peter H.", "clpid": "Lowy-P-H" } ], "abstract": "Nearly all experiments on the incorporation of labeled amino acids into tissue proteins in vitro have been done on tissues whose cell structure has been partially or completely disintegrated, e.g. tissue slices, segments, or homogenates. Since cell destruction reduces or abolishes the uptake of labeled amino acids (1), it seemed worth while to carry out studies on intact cells in vitro. Bone marrow cells were found to be suitable for this purpose. The labeled amino acids used were glycine-1-C14, L-leucine-1-C14, L-lysine-1-C14, and L-lysine-6-C14.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1950-09", "series_number": "1", "volume": "186", "issue": "1", "pages": "297-307" }, { "id": "authors:292qq-tbg35", "collection": "authors", "collection_id": "292qq-tbg35", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc50b", "type": "article", "title": "Incorporation in vitro of labeled amino acids into rat diaphragm proteins", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Deasy", "given_name": "Clara L.", "clpid": "Deasy-C-L" }, { "family_name": "Haagen-Smit", "given_name": "A. J.", "clpid": "Haagen-Smit-A-J" }, { "family_name": "Keighley", "given_name": "Geoffrey", "clpid": "Keighley-G" }, { "family_name": "Lowy", "given_name": "Peter H.", "clpid": "Lowy-P-H" } ], "abstract": "We have reported the incorporation of labeled amino acids into the proteins of rabbit bone marrow cells in vitro (1), a study that was undertaken to compare the process in intact cells as compared with tissue slices and homogenates. Bone marrow cells are a mixture in different stages of maturity. The uptake of labeled amino acids by rat diaphragm was studied because it is an adult tissue with predominantly one type of cell and it can be removed from the animal with little damage. This preparation has been found useful in studies of carbohydrate metabolism of muscle in vitro (2).", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1950-09", "series_number": "1", "volume": "186", "issue": "1", "pages": "309-315" }, { "id": "authors:akpb3-2nn23", "collection": "authors", "collection_id": "akpb3-2nn23", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc50a", "type": "article", "title": "The uptake in vitro of C14-labeled glycine, L-leucine, and L-lysine by different components of guinea pig liver homogenate", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Deasy", "given_name": "Clara L.", "clpid": "Deasy-C-L" }, { "family_name": "Haagen-Smit", "given_name": "A. J.", "clpid": "Haagen-Smit-A-J" }, { "family_name": "Keighley", "given_name": "Geoffrey", "clpid": "Keighley-G" }, { "family_name": "Lowy", "given_name": "Peter H.", "clpid": "Lowy-P-H" } ], "abstract": "We have reported (1) that L-lysine labeled with C14 can be incorporated into the proteins of guinea pig liver homogenate under two different conditions. In the one case the enzyme used was the whole homogenate, the optimum pH was near 6.2, there was an obligatory requirement of calcium, and the incorporation was independent of oxygen. This set of conditions is designated below as the \"acid calcium\" condition. In the other case the enzyme system was the precipitate obtained by centrifuging the homogenate diluted 15-fold with Ringer's solution at 2500 X g, the optimum pH was near to 7.3, the reaction was accelerated a little by calcium but the presence of calcium was not obligatory, and the incorporation was a little less under nitrogen than under oxygen. This set of conditions is designated below as the \"alkaline\" condition.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1950-06", "series_number": "2", "volume": "184", "issue": "2", "pages": "529-543" }, { "id": "authors:k8ze4-a2j60", "collection": "authors", "collection_id": "k8ze4-a2j60", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc49a", "type": "article", "title": "The incorporation of labeled lysine into the proteins of guinea pig liver homogenate", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Deasy", "given_name": "Clara L.", "clpid": "Deasy-C-L" }, { "family_name": "Haagen-Smit", "given_name": "A. J.", "clpid": "Haagen-Smit-A-J" }, { "family_name": "Keighley", "given_name": "Geoffrey", "clpid": "Keighley-G" }, { "family_name": "Lowy", "given_name": "Peter H.", "clpid": "Lowy-P-H" } ], "abstract": "When C14-labeled lysine is incubated with guinea pig liver homogenate, \u03b1-aminoadipic, \u03b1-ketoadipic, and glutaric acids are formed from the lysine (1). These transformations were established by finding the radioactivity of the C14 tracer in the metabolic products. The homogenate proteins coagulated by boiling at pH 5 also contained radioactivity. The counts given by the proteins corresponded to about 0.02 to 0.03 per cent of that added as lysine; the extent of lysine incorporation into the proteins was of the same order of magnitude as Melchior and Tarver (2) had found after incubating S35-labeled methionine and Winnick et al. (3, 4) C14-labeled glycine with rat tissue homogenates. Yet we could not satisfy ourselves that the radioactivity remaining in the proteins in our experiments, although it persisted through exhaustive extraction, did not come from traces of adsorbed radioactive lysine. Some counts were found in the protein when the homogenate was boiled prior to incubation with isotopic lysine.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1949-06-01", "series_number": "2", "volume": "179", "issue": "2", "pages": "689-704" }, { "id": "authors:mgqcq-zqs17", "collection": "authors", "collection_id": "mgqcq-zqs17", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc49b", "type": "article", "title": "A peptide fraction in liver", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Deasy", "given_name": "Clara L.", "clpid": "Deasy-C-L" }, { "family_name": "Haagen-Smit", "given_name": "A. J.", "clpid": "Haagen-Smit-A-J" }, { "family_name": "Keighley", "given_name": "Geoffrey", "clpid": "Keighley-G" }, { "family_name": "Lowy", "given_name": "Peter H.", "clpid": "Lowy-P-H" } ], "abstract": "We reported in a preliminary communication (1) the isolation of a peptide fraction from guinea pig liver. The following points of interest appeared at once: many different amino acids were obtained on hydrolysis; the peptide fraction contained most of the indispensable amino acids, which indicated that it probably is important in protein metabolism; when guinea pig liver homogenate was incubated with C14-labeled glycine, leucine, or lysine, these were rapidly incorporated into this peptide fraction, which is further evidence that it is metabolically active; the peptide fraction had not been described hitherto; a fraction containing one or more large peptides can be separated from so complex a mixture as liver homogenate by starch chromatography.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1949-06-01", "series_number": "2", "volume": "179", "issue": "2", "pages": "705-719" }, { "id": "authors:heqje-85r32", "collection": "authors", "collection_id": "heqje-85r32", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc48c", "type": "article", "title": "The degradation of L-lysine in guinea pig liver homogenate: formation of alpha-aminoadipic acid", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Deasy", "given_name": "Clara L.", "clpid": "Deasy-C-L" }, { "family_name": "Haagen-Smit", "given_name": "A. J.", "clpid": "Haagen-Smit-A-J" }, { "family_name": "Keighley", "given_name": "Geoffrey", "clpid": "Keighley-G" }, { "family_name": "Lowy", "given_name": "Peter H.", "clpid": "Lowy-P-H" } ], "abstract": "A summary of the little that is known of the metabolism of lysine in animals is as follows: it is indispensable in the diet, its \u03b1-amino group does not participate in reversible transamination reaction in vivo (2), neither the L nor D form is attacked by the appropriate amino acid oxidase, certain \u03b5-nitrogen-substituted derivatives can replace lysine in the diet and their \u03b1-amino groups are oxidized by amino acid oxidases (3, 4), no \u03b1-nitrogen-substituted derivatives yet prepared can substitute for lysine in the diet (4-6).", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1948-12-01", "series_number": "3", "volume": "176", "issue": "3", "pages": "1383-1393" }, { "id": "authors:s8dn1-nzt25", "collection": "authors", "collection_id": "s8dn1-nzt25", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc48d", "type": "article", "title": "The degradation of alpha-aminoadipic acid in guinea pig liver homogenate", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Deasy", "given_name": "Clara L.", "clpid": "Deasy-C-L" }, { "family_name": "Haagen-Smit", "given_name": "A. J.", "clpid": "Haagen-Smit-A-J" }, { "family_name": "Keighley", "given_name": "Geoffrey", "clpid": "Keighley-G" }, { "family_name": "Lowy", "given_name": "Peter H.", "clpid": "Lowy-P-H" } ], "abstract": "In continuation of our study of the metabolism of L-lysine, \u03b1-aminoadipic acid, which is formed from lysine in guinea pig liver homogenate (1), was synthesized with C14 in the \u03b5-position. The metabolism of the latter compound was followed by search for the radioactive tracer among the probable metabolic products. Two have been identified, \u03b1-ketoadipic and glutaric acids.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1948-12", "series_number": "3", "volume": "176", "issue": "3", "pages": "1395-1400" }, { "id": "authors:f9ack-w5h64", "collection": "authors", "collection_id": "f9ack-w5h64", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:DUBjbc48b", "type": "article", "title": "Dimethylthetin and dimethyl-\u03b2-propriothetin in methionine synthesis", "author": [ { "family_name": "Dubnoff", "given_name": "Jacob W.", "clpid": "Dubnoff-J-W" }, { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" } ], "abstract": "In a previous communication it was shown that choline and betaine are effective in promoting methionine synthesis from homocysteine in tissue homogenates (1). Data presented in this paper indicate that dimethylthetin, (CH3)2+SCH2COO-, which has been shown by Welch (2) to be lipotropic and has been reported by du Vigneaud (3) to promote growth on a methionine-free, homocysteine-containing diet, is 20 times as active as betaine in methionine formation. Dimethyl-\u03b2-propiothetin, (CH3)2+S(CH2)2COO-, recently isolated from Polysiphonia fastigiata by Challenger and Simpson (4) is also highly active. The enzyme for this transmethylation is found in the liver and kidney of all animals tested. Its high activity and general distribution suggest its biological importance in methionine synthesis.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1948-11", "series_number": "2", "volume": "176", "issue": "2", "pages": "789-796" }, { "id": "authors:cgd70-13r86", "collection": "authors", "collection_id": "cgd70-13r86", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc48b", "type": "article", "title": "Isolation of a peptide in guinea pig liver homogenate and its turnover of leucine", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Deasy", "given_name": "Clara L.", "clpid": "Deasy-C-L" }, { "family_name": "Haagen-Smit", "given_name": "A. J.", "clpid": "Haagen-Smit-A-J" }, { "family_name": "Keighley", "given_name": "Geoffrey", "clpid": "Keighley-G" }, { "family_name": "Lowy", "given_name": "Peter H.", "clpid": "Lowy-P-H" } ], "abstract": "Leucine was synthesized with C14 in the carboxyl group. 10 mg. of the radioactive amino acid (DL) and 0.66 gm. (wet weight) of guinea pig liver homogenate were added to a reaction mixture containing 1.3 per cent of an amino acid mixture corresponding to the composition of casein and 0.005 M fumarate, all in a final volume of 4 ml. of isotonic saline solution(1) at pH 7.4. The reaction was carried out under oxygen for 6 hours at 38\u00b0.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1948-07-01", "series_number": "3", "volume": "174", "issue": "3", "pages": "1041-1042" }, { "id": "authors:3regx-w7c50", "collection": "authors", "collection_id": "3regx-w7c50", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc48a", "type": "article", "title": "Alpha-aminoadipic acid: A product of lysine metabolism", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Deasy", "given_name": "Clara L.", "clpid": "Deasy-C-L" }, { "family_name": "Haagen-Smit", "given_name": "A. J.", "clpid": "Haagen-Smit-A-J" }, { "family_name": "Keighley", "given_name": "Geoffrey", "clpid": "Keighley-G" }, { "family_name": "Lowy", "given_name": "Peter H.", "clpid": "Lowy-P-H" } ], "abstract": "As part of a study of protein and peptide metabolism lysine was synthesized with C14 in the \u03b5 position and resolved into the L and D isomers. 10 mg. of labeled lysine dihydrochloride (either L- or D-) and 0.66 gm. (wet weight) of guinea pig liver homogenate were added to a reaction mixture containing 1.3 per cent of an amino acid mixture corresponding to the composition of casein except for lysine and 0.01 M \u03b1-ketoglutarate, all in a final volume of 4 ml. of isotonic saline solution.(1) The reaction was carried out under oxygen for 6 hours at 38\u00b0.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1948-03", "series_number": "1", "volume": "173", "issue": "1", "pages": "423-424" }, { "id": "authors:ej6kp-42178", "collection": "authors", "collection_id": "ej6kp-42178", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:DUBjbc48a", "type": "article", "title": "\u03b1-aminoadipic acid in arginine formation", "author": [ { "family_name": "Dubnoff", "given_name": "Jacob W.", "clpid": "Dubnoff-J-W" }, { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" } ], "abstract": "The experiment presented in the table shows that \u03b1-aminoadipic acid can aminate citrulline, and that the relative reaction rates are compatible with the hypothesis that lysine is converted into \u03b1-aminoadipic acid.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1948-03", "series_number": "1", "volume": "173", "issue": "1", "pages": "425" }, { "id": "authors:e33fx-7rn16", "collection": "authors", "collection_id": "e33fx-7rn16", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc47f", "type": "article", "title": "On the role of the oxidation in the methylation of guanidoacetic acid", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Dubnoff", "given_name": "Jacob W.", "clpid": "Dubnoff-J-W" } ], "abstract": "There are two, at least, methyl transfer reactions promoted by liver slices in vitro (2). The fundamental distinction between them is that one is dependent on oxygen and the other is not.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1947-11", "series_number": "1", "volume": "171", "issue": "1", "pages": "363-375" }, { "id": "authors:g4jsg-gpx35", "collection": "authors", "collection_id": "g4jsg-gpx35", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc47c", "type": "article", "title": "Ornithine-catalyzed urea formation in liver homogenate", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Dubnoff", "given_name": "Jacob W.", "clpid": "Dubnoff-J-W" } ], "abstract": "Heretofore attempts to obtain synthesis of urea from ammonia (and carbon dioxide) in cell-free extracts have been unsuccessful. We have found the reaction to proceed in guinea pig liver homogenate. The following is the reaction mixture which has given the highest yields obtained so far: L-ornithine (0.00075 M), ammonia (0.0025 M), L-glutamate (0.01 M), oxalacetate (0.005 M), ATP (0.00025 M), and 0.33 gm. of homogenized liver in a final volume of 3.5 ml. The following are typical increases in urea over the blank observed in 1 hour, in micrograms: ornithine + ammonia 0, glutamate + oxalacetate 0, glutamate + oxalacetate + ornithine 49, glutamate + oxalacetate + ammonia 105, glutamate + oxalacetate + ornithine + ammonia 317, glutamate + ocalacetate + ornithine + ammonia (without ATP) 150.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1947-07-05", "series_number": "2", "volume": "169", "issue": "2", "pages": "461-462" }, { "id": "authors:zv4z2-1n888", "collection": "authors", "collection_id": "zv4z2-1n888", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc47e", "type": "article", "title": "Methionine formation by transmethylation in vitro", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Dubnoff", "given_name": "Jacob W.", "clpid": "Dubnoff-J-W" } ], "abstract": "We reported in a previous communication (1) that guanidoacetic acid is methylated to creatine by rat liver slices in the presence of choline and either homocysteine or homocystine. Choline, homocystine, or homocysteine alone had little or no effect. These observations closed the gap which had existed between the evidence from tissue slice experiments on the one hand (2) and that from experiments in viva on the other (3-5) regarding the transfer of choline methyl in the formation of creatine.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1947-07-01", "series_number": "2", "volume": "169", "issue": "2", "pages": "247-258" }, { "id": "authors:2jkew-x5010", "collection": "authors", "collection_id": "2jkew-x5010", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc47b", "type": "article", "title": "The hydrolysis of phosphocreatine and the origin of urinary creatinine", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Dubnoff", "given_name": "Jacob W.", "clpid": "Dubnoff-J-W" } ], "abstract": "Shaffer (1), Myers and Fine (2), and Hahn and Meyer (3) adduced evidence that muscle creatine is the precursor of urinary creatinine. This was questioned by Chanutin and Kinard (4) but was conclusively proved by Bloch, Schoenheimer, and Rittenberg (5, 6) by isotope tracer evidence, which also showed that creatinine was the only normal urinary constituent containing any significant amount of body creatine nitrogen (1).", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1947-05", "series_number": "2", "volume": "168", "issue": "2", "pages": "493-510" }, { "id": "authors:t4nda-fdp61", "collection": "authors", "collection_id": "t4nda-fdp61", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc47a", "type": "article", "title": "Synthesis of hippuric acid in liver homogenate", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Dubnoff", "given_name": "Jacob W.", "clpid": "Dubnoff-J-W" } ], "abstract": "The synthesis of hippuric acid from benaoic acid and glycine resembles in several respects the synthesis of a peptide bond. A CONH group is formed, it is a to a carboxyl group, and the free energy of its formation is of the same order of magnitude. The synthesis was demonstrated in liver and kidney slices of a number of animals; it is inhibited by 0.001 M KCN, which is in accord with the view that the necessary free energy is derived from an oxidation.(1)", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1947-04", "series_number": "1", "volume": "168", "issue": "1", "pages": "397-398" }, { "id": "authors:dkrcr-2r346", "collection": "authors", "collection_id": "dkrcr-2r346", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc45", "type": "article", "title": "Methylation of guanidoacetic acid by homocystine plus choline with rat liver slices", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Dubnoff", "given_name": "Jacob W.", "clpid": "Dubnoff-J-W" } ], "abstract": "The methylation of guanidoacetic acid by liver slices is accelerated by methionine; choline, under these conditions, exerts no significant accelerating effect (1). In view of the fact that homocystine plus choline can replace methionine for growth (2), and of the isotope experiments which proved the transfer in viva of the methyl groups of choline to creatine,(3) it has been suggested, from indirect evidence, that the pathway of the methyl group to creatine is more direct from methionine than from choline.(4) More specific evidence is desirable, especially as neither homocystine nor homocysteine has been identified in animal tissues.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1945-10", "series_number": "2", "volume": "160", "issue": "2", "pages": "635-636" }, { "id": "authors:j5kxf-jf802", "collection": "authors", "collection_id": "j5kxf-jf802", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc41c", "type": "article", "title": "The conversion of citrulline to arginine in kidney", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Dubnoff", "given_name": "Jacob W.", "clpid": "Dubnoff-J-W" } ], "abstract": "Glycocyamine is formed in the kidney by the transfer of the amidine group of arginine to the nitrogen atom of glycine. In the study of this reaction it was observed that glycocyamine was also formed from citrulline and glycine. No other donor or precursor of the amidine group was found (1).", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1941-12-01", "series_number": "3", "volume": "141", "issue": "3", "pages": "717-738" }, { "id": "authors:e06s1-prb22", "collection": "authors", "collection_id": "e06s1-prb22", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc41a", "type": "article", "title": "The formation of glycocyamine in man and its urinary excretion", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Dubnoff", "given_name": "Jacob W.", "clpid": "Dubnoff-J-W" }, { "family_name": "Lilly", "given_name": "John C.", "clpid": "Lilly-J-C" }, { "family_name": "Marriott", "given_name": "William", "clpid": "Marriott-W" } ], "abstract": "Glycocyamine was first isolated from human and dog urine and identified by Weber (1-3). He supported the view that glycocyamine is a normal precursor of creatine and that its appearance in urine (2) is \"an overflow phenomenon of an intermediate metabolic product ...\" He expressed no views on the mechanism of its formation.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1941-03", "series_number": "1", "volume": "138", "issue": "1", "pages": "405-410" }, { "id": "authors:zk7vw-r0z13", "collection": "authors", "collection_id": "zk7vw-r0z13", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc41b", "type": "article", "title": "The formation of glycocyamine in animal tissues", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Dubnoff", "given_name": "Jacob W.", "clpid": "Dubnoff-J-W" } ], "abstract": "It was shown in preceding communications that glycocyamine is converted into creatine by surviving liver slices (1). Our findings indicated that the methylating agent is methionine or a derivative of methionine. Liver slices can methylate glycocyamine rapidly enough to permit assignment to the liver alone, if necessary, of the task of making good the loss of creatine and creatinine in the urine. This holds for the livers of all mammals studied. We found no evidence of this methylating mechanism in any other tissues, except possibly slight activity in the kidney. In the pigeon the kidney is as effective in this respect as the liver.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1941-03", "series_number": "1", "volume": "138", "issue": "1", "pages": "389-403" }, { "id": "authors:7zfwr-hc735", "collection": "authors", "collection_id": "7zfwr-hc735", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:DUBjbc41a", "type": "article", "title": "A micromethod for the determination of glycocyamine in biological fluids and tissue extracts", "author": [ { "family_name": "Dubnoff", "given_name": "Jacob W.", "clpid": "Dubnoff-J-W" }, { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" } ], "abstract": "In the two following communications (1, 2) evidence is presented that glycocyamine is a normal precursor of creatine in the animal body. These studies required a satisfactory micromethod for the determination of glycocyamine. The most reliable method described in the literature consists in adsorption on Lloyd's reagent in acid solution, elution with baryta, removal of arginine from the eluate by repeated adsorption on permutit, and calorimetric determination of the remaining glycocyamine by means of the Sakaguchi reaction. There are only two substances which are common in biological fluids and which give an intense color in the Sakaguchi reaction. These are arginine and glycocyamine. This method was first introduced by Weber (3) and was modified by Bodansky (4) and by Davenport and Fisher (5). \n\nIn our hands even the latest version of the method, that described by Davenport and Fisher, had the following shortcomings: it was laborious and time-consuming, the adsorption of the glycocyamine on the Lloyd's reagent was incomplete, further losses of glycocyamine occurred in the repeated treatment with permutit (Davenport and Fisher report losing only 10 per cent in three adsorptions; with the permutit available to us we lost 80 per cent), and the color developed was unstable. Furthermore, the amount of glycocyamine lost on the permutit varied according to the amount of arginine present, the less arginine the greater the loss of glycocyamine. \n\nAll these disadvantages have been removed in the method described below. It is the first method in which glycocyamine added to blood or urine can be determined quantitatively, even in concentration8 as low a8 0.1 mg. per cent. 2 to 5 ml. are sufficient for an analysis. An indication of the speed and convenience of the method is that twenty to forty analyses can be carried through simultaneously in about 2 hours.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1941-03", "series_number": "1", "volume": "138", "issue": "1", "pages": "381-388" }, { "id": "authors:q6eft-85v12", "collection": "authors", "collection_id": "q6eft-85v12", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc40d", "type": "article", "title": "Creatine formation in liver and in kidney", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Dubnoff", "given_name": "Jacob W.", "clpid": "Dubnoff-J-W" } ], "abstract": "We reported recently (1) the formation of creatine from glycocyamine by rat liver slices; and that 40 to 50 per cent more creatine was formed when methionine was added with the glycocyamine to the Ringer's solution in which the slices were immersed. Among some thirty odd amino acids, methylated amines, a methylated purine, and betaine only methionine gave this increased rate of methylation. The rate of creatine formation under these conditions is sufficient, if it is of the same order of magnitude in vivo, to make good the entire loss as urinary creatinine.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1940-07", "series_number": "2", "volume": "134", "issue": "2", "pages": "635-639" }, { "id": "authors:3sznt-zps67", "collection": "authors", "collection_id": "3sznt-zps67", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORpnas40", "type": "article", "title": "The Course of Thiamin Metabolism in Man as Indicated by the Use of Radioactive Sulfur", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Buchman", "given_name": "Edwin R.", "clpid": "Buchman-E-R" }, { "family_name": "Hatcher", "given_name": "John B.", "clpid": "Hatcher-J-B" }, { "family_name": "Yost", "given_name": "Don M.", "clpid": "Yost-D-M" }, { "family_name": "McMillan", "given_name": "Edwin", "clpid": "McMillan-E" } ], "abstract": "When supplementary thiamin (Vitamin B1) is ingested or injected, the amount which appears in the urine during the succeeding twenty-four hours usually increases, but the total additional excretion always falls short of the supplement, even when the vitamin is injected and there can be no question of incomplete absorption. We have sought information on this unaccounted-for moiety by synthesizing thiamin from sulfur which contains the radioactive isotope S35 (designated as B1*) and by following, after injection of the B1*, the excretion of the radiosulfur (S*) in the urine and feces and the excretion of total free B1 in the urine.", "issn": "0027-8424", "publisher": "National Academy of Sciences", "publication": "Proceedings of the National Academy of Sciences of the United States of America", "publication_date": "1940-06-01", "series_number": "6", "volume": "26", "issue": "6", "pages": "412-418" }, { "id": "authors:xh38n-87a31", "collection": "authors", "collection_id": "xh38n-87a31", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc40c", "type": "article", "title": "The oxidation-reduction potential of coenzyme I", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" } ], "abstract": "The oxidation-reduction potential of cozymase (diphosphopyridine nucleotide) was calculated from the free energies of formation of aqueous d-alanine and d-glutamic acid based on thermal data, and the equilibria measured by Wurmser and Filitti-Wurmser(1) for pyruvate + 2H+ + 2(e) \u21cc alanine + H2O, by Cohen(2) for \u03b1-ketoglutarate + alanine \u21cc d-glutamate and pyruvate, and by von Euler et al.(3) for the reaction \u03b1-ketoglutarate + NH+4 + reduced cozymase \u21cc glutamate + oxidized cozymase. The value for the potential so calculated is at 30\u00b0 E'0 = -0.072 - 0.03 pH \u00b1 0.0008 volt.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1940-04", "series_number": "2", "volume": "133", "issue": "2", "pages": "629-630" }, { "id": "authors:6rp92-ap183", "collection": "authors", "collection_id": "6rp92-ap183", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc40b", "type": "article", "title": "The formation of creatine from glycocyamine in the liver", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Dubnoff", "given_name": "Jacob W.", "clpid": "Dubnoff-J-W" } ], "abstract": "The study of the precursors of creatine in animals has been beset by two difficulties principally. One has been the lack of really adequate biological material; the other, the lack of a specific, and at the same time sensitive analytical method. Experiments hitherto have consisted in attempts to change the urinary excretion of creatine and creatinine, or the creatine content of the tissues of intact animals or of isolated perfused organs. The normal, i.e. uncontrolled, fluctuations in tissue composition and urinary excretion are relatively large compared with the changes induced experimentally; it is often impossible to distinguish when experimental effects are observed, whether these have arisen from changes in the processes of excretion or synthesis; there may be variations in the water content of the tissues, thereby affecting their percentile composition; all of these have stood in the way of firm conclusions being drawn.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1940-02", "series_number": "2", "volume": "132", "issue": "2", "pages": "559-574" }, { "id": "authors:kecdd-b4t60", "collection": "authors", "collection_id": "kecdd-b4t60", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc40a", "type": "article", "title": "The biological synthesis of hippuric acid in vitro", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Dubnoff", "given_name": "Jacob W.", "clpid": "Dubnoff-J-W" } ], "abstract": "The mechanism of the synthesis of hippuric acid in viva is interesting from several points of view. There is the intrinsic interest in a compound found in the urine of many animals, an interest which is heightened by the use of the rate of hippuric acid excretion following the administration of benzoic acid as a clinical test of liver function. This synthesis is interesting also from the point of view of physiological energetics. The formation of hippuric acid from glycine and benzoic acid is attended by a gain in free energy (Table I). In other words the tendency of the reaction, if allowed to proceed spontaneously at 25\u00b0 or 38\u00b0, is not toward synthesis but toward practically complete hydrolysis of hippuric acid (Table III). Yet when benzoic acid is fed, hippuric acid is rapidly synthesized. This synthesis also occurs and can be measured, as shown below, when liver slices are suspended in Ringer's solution containing low concentrations of benzoic acid and glycine. More than half the benzoic acid is converted to hippuric acid. From the thermodynamic data it may be deduced that the enzymatic synthesis of hippuric acid cannot be simply the reverse of its hydrolysis. The hydrolysis can proceed spontaneously; the synthesis must be coupled with an energy-yielding reaction.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1940-01", "series_number": "1", "volume": "132", "issue": "1", "pages": "307-324" }, { "id": "authors:70v5n-eyv89", "collection": "authors", "collection_id": "70v5n-eyv89", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc39", "type": "article", "title": "Methods for the determination of submicro quantities of total nitrogen, ammonia, amino nitrogen, amides, peptides, adenylic acid, and nitrates", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Dubnoff", "given_name": "Jacob W.", "clpid": "Dubnoff-J-W" } ], "abstract": "In 1935 one of us described micromethods for ammonia, urea, total nitrogen, uric acid, creatinine, and allantoin (1). These methods are adapted for the analysis of 1 to 2 ml. aliquots of dilute solutions, e.g. 0.1 mg. per cent of ammonia or urea, and for carrying out a large number of analyses simultaneously. These methods all end in a calorimetric measurement.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1939-11", "series_number": "1", "volume": "131", "issue": "1", "pages": "163-176" }, { "id": "authors:nfyca-c2972", "collection": "authors", "collection_id": "nfyca-c2972", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc37a", "type": "article", "title": "The oxidation of ascorbic acid and its reduction in vitro and in vivo", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Davenport", "given_name": "Horace W.", "clpid": "Davenport-H-W" }, { "family_name": "Jeffreys", "given_name": "Cecil E. P.", "clpid": "Jeffreys-C-E-P" }, { "family_name": "Warner", "given_name": "Robert C.", "clpid": "Warner-R-C" } ], "abstract": "The outstanding chemical property of ascorbic acid (vitamin C) is that it is a reducing agent. The suggestion is obvious that its physiological function may be associated with this property, and, if it is oxidized reversibly, with its behavior in an oxidation-reduction system. It is desirable therefore to know the oxidation-reduction potential of ascorbic acid.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1937-01-01", "series_number": "1", "volume": "117", "issue": "1", "pages": "237-279" }, { "id": "authors:d0fz5-45w87", "collection": "authors", "collection_id": "d0fz5-45w87", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc37b", "type": "article", "title": "Sulfhydryl oxidation-reduction potentials derived from thermal data", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Ellis", "given_name": "Emory L.", "clpid": "Ellis-E-L" }, { "family_name": "Huffman", "given_name": "Hugh M.", "clpid": "Huffman-H-M" } ], "abstract": "The isolation of glutathione by Hopkins in 1921 and his experiments suggesting that this compound is probably an intermediary in biological oxidations and reductions awakened an active interest in the biological significance of sulfhydryl compounds in general (1, 2). Among the fundamental data pertaining to these compounds are their oxidation-reduction potentials. Soon after the discovery of glutathione a number of attempts were made to measure these potentials by electrometric and calorimetric methods. In all except the most recent investigations the potential observed in aqueous solutions with noble metal electrodes was independent of the concentration of the oxidized form (R\u2014S\u2014S\u2014R) (3-5).", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1937-01", "series_number": "1", "volume": "117", "issue": "1", "pages": "281-308" }, { "id": "authors:7d86b-b5b94", "collection": "authors", "collection_id": "7d86b-b5b94", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc35b", "type": "article", "title": "Nitrogen metabolism of the isolated tissues of the rat", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Jeffreys", "given_name": "Cecil E. P.", "clpid": "Jeffreys-C-E-P" } ], "abstract": "Little study has been devoted to the anabolic aspects of nitrogen metabolism in animals. The reason, of course, has been the difficulty of obtaining experimental conditions in which these can be observed, measured, and analyzed. The experiments of Krebs and Henseleit (1) on the formation of urea from ammonia with Warburg's method of surviving slices of liver suggested that this method might be useful in a direct attack on a number of problems of nitrogen anabolism in animals; i.e., it might be possible to observe reactions in which there is a gain in free energy. It appears that for these reactions the intact cell structure is necessary.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1935-07-01", "series_number": "2", "volume": "110", "issue": "2", "pages": "495-509" }, { "id": "authors:23qbq-7xe96", "collection": "authors", "collection_id": "23qbq-7xe96", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORpnas35", "type": "article", "title": "The correlation between excess calories and excess urinary nitrogen in the specific dynamic action of protein in animals", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" } ], "abstract": "Several years ago it was pointed out that after the ingestion of proteins or amino acids a definite correlation existed between the calories and urinary nitrogen in excess of the basal(1) The data used were those obtained by Rapport,(2) Weiss and Rapport(3) and Rapport and Beard.(4) Aubel and Schaeffer(5) were of the opinion that this correlation bears no relation to the specific dynamic action of protein and amino acids. Their main reason was that the curves of extra calories and extra nitrogen are not synchronous; that the curve of caloric metabolism returns to the basal level before that of the nitrogen.", "doi": "10.1073/pnas.21.7.492", "issn": "0027-8424", "publisher": "National Academy of Sciences", "publication": "Proceedings of the National Academy of Sciences of the United States of America", "publication_date": "1935-07-01", "series_number": "7", "volume": "21", "issue": "7", "pages": "492-498" }, { "id": "authors:jmn8a-5v003", "collection": "authors", "collection_id": "jmn8a-5v003", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc35a", "type": "article", "title": "Micromethods for determination of ammonia, urea, total \n nitrogen, uric acid, creatinine (and creatine), and allantoin", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" } ], "abstract": "The success with which Krebs and Henseleit (1) employed Warburg's method of surviving tissue slices in the problem of the formation of urea in the liver encouraged its use for a direct attack on other problems of nitrogen metabolism in animals.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1935-07", "series_number": "2", "volume": "110", "issue": "2", "pages": "481-493" }, { "id": "authors:ga3mh-j3m52", "collection": "authors", "collection_id": "ga3mh-j3m52", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORpnas34", "type": "article", "title": "A Theory of Protein Metabolism in Man", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Keighley", "given_name": "Geoffrey", "clpid": "Keighley-G" } ], "abstract": "During a 24-hour period when the subject is maintained in nitrogen balance with either protein, or a mixture of amino acids, or a single amino acid, the larger fraction (60-75%) of the nitrogen metabolized in this period is derived not from the nitrogen ingested during this interval, but from that already present. In this sense the bulk of the protein metabolized in any one day is endogenous. The term endogenous is used here in a different sense from the connotation given it by Folin, who used it to designate the wear and tear quota of protein metabolized. The simplest direct evidence for the above conclusion was furnished by experiments in which a mixture of amino acids and protein was ingested containing only a small amount of sulphur. These experiments showed that under these conditions there is no sparing of the basal sulphur. In several instances more sulphur was excreted than the sum of the amount ingested and the total excreted during a fasting period of 24 hours. It follows therefore that when protein is ingested the nitrogen and sulphur excreted do not come for the most part from the ingested protein; but that approximately three quarters is derived from protein (or protein split products) already in the organism.", "issn": "0027-8424", "publisher": "National Academy of Sciences", "publication": "Proceedings of the National Academy of Sciences of the United States of America", "publication_date": "1934-03-01", "series_number": "3", "volume": "20", "issue": "3", "pages": "179-183" }, { "id": "authors:1rqp8-ndq97", "collection": "authors", "collection_id": "1rqp8-ndq97", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc33b", "type": "article", "title": "The preparation of crystalline lactic acid", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Huffman", "given_name": "Hugh M.", "clpid": "Huffman-H-M" }, { "family_name": "Liu", "given_name": "Yun-Pu", "clpid": "Liu-Yun-Pu" } ], "abstract": "On account of its importance in intermediary metabolism, lactic acid was among the first compounds chosen in our plan, which we have described in a previous communication (1), to augment the available data on the free energies of formation of substances significant in biological chemistry. It was necessary for this purpose to obtain pure crystalline lactic acid, free of water, anhydride, and lactide. The only description in the literature of the preparation of crystalline lactic acid is that of Krafft and D\u00ffes (2). Table I shows that the product obtained by their method contains relatively large quantities of anhydro impurities. The subject of the present communication is the description of a method which yields the active isomers of lactic acid in a crystalline state, free of water, anhydride, and lactide, supplemented by the description of two methods of separating the active forms from the commercial syrup (1). Lactic acid commercially available at present either is in the form of the U.S.P. syrup, which usually exhibits a low optical activity corresponding to the excess it happens to contain, which is variable, of one or the other optical isomer, or is the expensive zinc sarcolactate. The methods described below now make it possible to obtain easily and quickly and at low cost large quantities of both active isomers in a relatively high degree of purity.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1933-10", "series_number": "2", "volume": "102", "issue": "2", "pages": "449-460" }, { "id": "authors:fk2tn-6c855", "collection": "authors", "collection_id": "fk2tn-6c855", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORpnas33", "type": "article", "title": "Oxidation reduction potential of ascorbic acid (Vitamin C)", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Keighley", "given_name": "Geoffrey", "clpid": "Keighley-G" } ], "abstract": "The measurement of the oxidation-reduction potential of ascorbic acid (Vitamin C) is desirable in the elucidation of its physiological action. Two attempts have been made to measure this potential. Georgescu(1) concluded that he had obtained a thermodynamically reversible potential at pH 6.9, and 7.0 at 20\u00b0C. From the data presented, however, it is not possible to accept this interpretation without reservation.", "issn": "0027-8424", "publisher": "National Academy of Sciences", "publication": "Proceedings of the National Academy of Sciences of the United States of America", "publication_date": "1933-09-01", "series_number": "9", "volume": "19", "issue": "9", "pages": "875-878" }, { "id": "authors:wp6gj-j1723", "collection": "authors", "collection_id": "wp6gj-j1723", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORpnas33a", "type": "article", "title": "The Energy of Urea Synthesis. II. The Effect of Varying Hydrogen Ion Concentration with Different Metabolites", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Keighley", "given_name": "Geoffrey", "clpid": "Keighley-G" } ], "abstract": "In a previous communication [1] we have reported that an increased oxygen consumption can be observed accompanying the synthesis of urea by liver slices from ammonium bicarbonate. This observation is now confirmed, and the results of additional experiments are presented which elucidate to some extent some of the general features of the mechanism of the transfer of energy in this and probably other coupled reactions.", "issn": "0027-8424", "publisher": "National Academy of Sciences", "publication": "Proceedings of the National Academy of Sciences of the United States of America", "publication_date": "1933-07-01", "series_number": "7", "volume": "19", "issue": "7", "pages": "720-725" }, { "id": "authors:ryj8w-72204", "collection": "authors", "collection_id": "ryj8w-72204", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORpnas33b", "type": "article", "title": "The Energy of Urea Synthesis", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Keighley", "given_name": "Geoffrey", "clpid": "Keighley-G" } ], "abstract": "This study of the energy changes accompanying the synthesis of urea by living tissue from ammonia and carbon dioxide was undertaken in order to obtain more information regarding the causes of the specific dynamic action of protein; and because this reaction seems to be particularly suitable for the study of the energy changes in biological coupled reactions. In the synthesis of urea from ammonia and carbon dioxide (in which a large fraction of the ammonia is converted) there is a gain in free energy, which can be derived only from some other free energy liberating reaction.", "issn": "0027-8424", "publisher": "National Academy of Sciences", "publication": "Proceedings of the National Academy of Sciences of the United States of America", "publication_date": "1933-06-01", "series_number": "6", "volume": "19", "issue": "6", "pages": "626-631" }, { "id": "authors:nmtst-zcy59", "collection": "authors", "collection_id": "nmtst-zcy59", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc33a", "type": "article", "title": "The free energies of formation of aqueous d-alanine, l-aspartic acid, and d-glutamic acid", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Huffman", "given_name": "Hugh M.", "clpid": "Huffman-H-M" } ], "abstract": "The employment of thermodynamics in biochemistry has been restricted, until recently, to the use of first law data. In the last few years a beginning has been made in the application of the second law; i.e., of free energy data (1, 2). The development of this field is limited by the paucity of available free energy data. We have therefore undertaken the systematic determination of the free energies of formation of compounds which may be interesting in biochemistry or physiology.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1933-02", "series_number": "3", "volume": "99", "issue": "3", "pages": "663-676" }, { "id": "authors:2xy73-5gb77", "collection": "authors", "collection_id": "2xy73-5gb77", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc32", "type": "article", "title": "The cupric complexes of glycine and of alanine", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Thimann", "given_name": "Kenneth V.", "clpid": "Thimann-K-V" } ], "abstract": "The following report is the first of a projected series of studies of the physical chemistry of the compounds of the heavy metals, particularly of copper and of iron, with substances of biological importance. These studies are invited by the accumulation in recent years of examples of the importance of the heavy metals in biological chemistry.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1932-11", "series_number": "2", "volume": "98", "issue": "2", "pages": "671-705" }, { "id": "authors:09c68-nza82", "collection": "authors", "collection_id": "09c68-nza82", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc31a", "type": "article", "title": "The role of the enzyme in the succinate-enzyme-fumarate equilibrium", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Schott", "given_name": "Hermann F.", "clpid": "Schott-H-F" } ], "abstract": "The following is an account of an investigation into the role of the enzyme in the succinate-enzyme-fumarate equilibrium. The method consisted in the comparison of the value of the free energy change in this reaction obtained from oxidation-reduction potentials, with that calculated from the entropies and other physicochemical properties of succinic acid and fumaric acid.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1931-08", "series_number": "3", "volume": "92", "issue": "3", "pages": "535-557" }, { "id": "authors:c96yb-ern05", "collection": "authors", "collection_id": "c96yb-ern05", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc31b", "type": "article", "title": "The free energy, heat, and entropy of formation of l-malic acid", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Schott", "given_name": "Hermann F.", "clpid": "Schott-H-F" } ], "abstract": "In the previous communication (1), it was shown that the free energy of the bivalent fumarate ion at 25\u00b0 is -144,630 calories. In the present communication the measurement of the equilibrium at 25\u00b0 between fumaric acid and malic acid in the presence of fumarase is reported, and from the values obtained computations are made of the free energy and heat of formation of the bivalent l-malate ion and of the free energy and entropy of solid l-malic acid.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1931-08", "series_number": "3", "volume": "92", "issue": "3", "pages": "559-567" }, { "id": "authors:fhhsj-ne026", "collection": "authors", "collection_id": "fhhsj-ne026", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORpnas33c", "type": "article", "title": "On the Specific Dynamic Action of Protein", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Winegarden", "given_name": "Howard M.", "clpid": "Winegarden-H-M" } ], "abstract": "The purpose of the present communication is to show that the course of the specific dynamic action of protein parallels the course of nitrogen excretion; and in the well-nourished animal is the result of at least two processes, of which one is the work imposed upon the kidney, and the other is what may be called the \"specific dynamic action proper,\" due to the metabolism other than excretion of the nitrogen, and of the carbon.", "issn": "0027-8424", "publisher": "National Academy of Sciences", "publication": "Proceedings of the National Academy of Sciences of the United States of America", "publication_date": "1931-02-01", "series_number": "2", "volume": "17", "issue": "2", "pages": "75-91" }, { "id": "authors:eg714-41p55", "collection": "authors", "collection_id": "eg714-41p55", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORpnas31a", "type": "article", "title": "The Work of the Kidney in the Production of Urine", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Winegarden", "given_name": "Howard M.", "clpid": "Winegarden-H-M" } ], "abstract": "The work performed by the kidney in the production of urine appears to be more readily susceptible of analysis by means of the laws of thermodynamics than any other complete function of the animal body. The recognition of this possibility, of course, is not new. It has attracted a number of investigators whose essays have been collected and reviewed by Cushny [1]. The purpose and method were essentially the same in all of these studies: the computation of the theoretical minimum amount of work necessary to elaborate a solution such as urine from another such as blood. None of these computations was complete; and even in the last, made in 1914 [2], a number of processes were not taken into account, viz.: the suppression of ionization of the phosphates, and other weak acids by the greater acidity of the urine, and the production of ammonia from urea by the kidney. \n\nIn the account presented below of the minimum work necessary for the production of the urine, an attempt has been made to appraise the factors omitted in previous studies; and an alternative method has been employed in the analysis of the work involved in the transport of water. It is felt that a clearer understanding of the energetics of water transport in the body in general is obtained from the alternative treatment. The minimum work has been considered as a quantity equal to the sum of the free energy changes for the transport of each constituent, including water, from blood to urine. It has been assumed, an assumption justifiable on practical grounds, that the substances concerned may be considered as perfect solutes.", "issn": "0027-8424", "publisher": "National Academy of Sciences", "publication": "Proceedings of the National Academy of Sciences of the United States of America", "publication_date": "1931-01-01", "series_number": "1", "volume": "17", "issue": "1", "pages": "3-12" }, { "id": "authors:3p42f-xj442", "collection": "authors", "collection_id": "3p42f-xj442", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORpnas31b", "type": "article", "title": "The Energy Cost of the Excretion of Urine", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Winegarden", "given_name": "Howard M.", "clpid": "Winegarden-H-M" } ], "abstract": "The energy consumption of the kidney has been estimated by a number of experimenters and by different methods; and the values obtained are all of the same order of magnitude. The concordance of these values justifies an estimate of the efficiency of the kidney, i.e., of the ratio of the work performed, calculated from the constitution of the urine, to the energy used. The efficiency of the kidney, defined in this way, appears, even in health, to be about 1-2 per cent. So far as the authors are aware, there are no data inconsistent with this low figure. Rather the reverse, this association of the thermodynamic work with the observed energy consumption of the kidney permits the correlation of a large number of facts regarding the behavior of the kidney in health and disease.", "issn": "0027-8424", "publisher": "National Academy of Sciences", "publication": "Proceedings of the National Academy of Sciences of the United States of America", "publication_date": "1931-01-01", "series_number": "1", "volume": "17", "issue": "1", "pages": "13-28" }, { "id": "authors:tjg8j-mhy83", "collection": "authors", "collection_id": "tjg8j-mhy83", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORpnas30", "type": "article", "title": "On the free energy of glucose and of tripalmitin", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Winegarden", "given_name": "Howard M.", "clpid": "Winegarden-H-M" } ], "abstract": "The theoretical maximum amount of work derivable from a chemical reaction is a quantity which we may designate as the reversible work, and which is equal to the decrease in the free energy of the system plus the change in the pressure-volume product. In the form of an equation this is: WR = -\u25b2F + \u25b2(PV).", "issn": "0027-8424", "publisher": "National Academy of Sciences", "publication": "Proceedings of the National Academy of Sciences of the United States of America", "publication_date": "1930-09-01", "series_number": "9", "volume": "16", "issue": "9", "pages": "559-573" }, { "id": "authors:3hbgk-w7j70", "collection": "authors", "collection_id": "3hbgk-w7j70", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjgp30b", "type": "article", "title": "The effect of isoelectric amino acids on the pH(+) of a phosphate buffer solution - A contribution in support of the \"Zwitter Ion\" hypothesis", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "MacFadyen", "given_name": "Douglas A.", "clpid": "MacFadyen-D-A" } ], "abstract": "The relative merits of the classical conception and of the Zwitter Ion conception of the dissociation of amphoteric electrolytes are discussed, and the following data are presented which confirm the Zwitter Ion hypothesis of Bjerrum, and which are not in accord with the classical view. \n\n1. Amino acids in the isoelectric form resemble strong electrolytes in that they contribute to the ionic strength of the solution. \n\n2. The dielectric constants of aqueous solutions of amino acids, like those of solutions of strong electrolytes greater than 0.02 normal, are considerably greater than that of pure water. \n\n3. The magnitude of the dissociation constants of substituted acetic acids and of glycine, are more easily accounted for with the Zwitter Ion than with the classical conception.", "doi": "10.1085/jgp.13.5.509", "pmcid": "PMC2141070", "issn": "0022-1295", "publisher": "Rockefeller University Press", "publication": "Journal of General Physiology", "publication_date": "1930-05", "series_number": "5", "volume": "13", "issue": "5", "pages": "509-527" }, { "id": "authors:5wscg-z7p95", "collection": "authors", "collection_id": "5wscg-z7p95", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:20140902-143707272", "type": "article", "title": "The enzymatic synthesis of protein", "author": [ { "family_name": "Wasteneys", "given_name": "Hardolph", "clpid": "Wasteneys-H" }, { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" } ], "abstract": "The study of enzymatic synthesis is of especial interest in the case\nof the proteins because of the great complexity and size of protein molecules\nas compared with other biologically important chemical groups\nsuch as carbohydrates and fats, and because of the intrinsic importance\nof protein synthesis in the building up and maintenance of the structure\nof the organism.", "issn": "0031-9333", "publisher": "American Physiological Society", "publication": "Physiological Reviews", "publication_date": "1930-01", "series_number": "1", "volume": "10", "issue": "1", "pages": "110-145" }, { "id": "authors:3gd5g-j7921", "collection": "authors", "collection_id": "3gd5g-j7921", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjgp30a", "type": "article", "title": "The substrate in peptic synthesis of protein", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "MacFadyen", "given_name": "Douglas A.", "clpid": "MacFadyen-D-A" }, { "family_name": "Wasteneys", "given_name": "Hardolph", "clpid": "Wasteneys-H" } ], "abstract": "Experiments are described in which it was observed that the yield of protein that can be synthesized by pepsin from a given peptic digest is highest when the hydrolyzing action of the pepsin is stopped as soon as all the protein has disappeared from the solution; and that the longer the digest is permitted to contain active enzyme the more the yield diminishes. \n\n2. Exposure of the digest to a hydrogen ion concentration of pH 1.6 in the absence of active enzyme, does not cause a diminution in the amount of protein which can be synthesized from that digest. \n\n3. Synthesis can be effected also in concentrated solutions of isolated fractions of a peptic digest, i.e. of proteose and of peptone. The yields are approximately the same as in similar concentrations of the whole digest, though the proteins so synthesized differ in some respects from those obtained from the whole digest. \n\n4. The cessation of synthesis in any one digest is due to the attainment of equilibrium and not to the complete utilization of available synthesizeable material. The amount of the equilibrium yield, on the other hand, is dependent on the amount of synthesizeable material in the digest. \n\n5. These observations are taken to show that the synthesizeability of a given mixture of protein cleavage products by pepsin depends upon its possession of a special complex in these products. This complex appears as a result of the primary hydrolysis of the protein molecule by pepsin and is decomposed in the slow secondary hydrolysis which ensues as digestion is prolonged.", "doi": "10.1085/jgp.13.3.295", "pmcid": "PMC2141042", "issn": "0022-1295", "publisher": "Rockefeller University Press", "publication": "Journal of General Physiology", "publication_date": "1930-01", "series_number": "3", "volume": "13", "issue": "3", "pages": "295-306" }, { "id": "authors:xadbx-rre30", "collection": "authors", "collection_id": "xadbx-rre30", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:20140807-143747458", "type": "article", "title": "The influence of the backward reaction in the peptic hydrolysis of albumin", "author": [ { "family_name": "Morrell", "given_name": "Clarence A.", "clpid": "Morrell-C-A" }, { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Wasteneys", "given_name": "Hardolph", "clpid": "Wasteneys-H" } ], "abstract": "1. No destruction of pepsin by heat is demonstrable at pH 1.6 until a temperature of 40\u00b0C. is exceeded.\n\n2. The influence of the backward reaction in peptic hydrolysis is shown in the diminishing rate at which increasing concentrations of protein are hydrolyzed. \n\n3. The backward reaction causes the optimum for the hydrolysis of higher concentrations of protein to be attained at a lower temperature than with more dilute solutions. \n\n4. The proteose and peptone associated with commercial pepsin retard hydrolysis in the same sense as the products due to the action of the enzyme.", "doi": "10.1085/jgp.8.6.601", "pmcid": "PMC2140816", "issn": "0022-1295", "publisher": "Rockefeller University Press", "publication": "Journal of General Physiology", "publication_date": "1927-03", "series_number": "6", "volume": "8", "issue": "6", "pages": "601-617" }, { "id": "authors:40d5e-8w676", "collection": "authors", "collection_id": "40d5e-8w676", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:20131204-160039218", "type": "article", "title": "The autodestruction of pepsin in relation to its ionization", "author": [ { "family_name": "Goulding", "given_name": "Arthur M.", "clpid": "Goulding-A-M" }, { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Wasteneys", "given_name": "Hardolph", "clpid": "Wasteneys-H" } ], "abstract": "1. Evidence is presented that pepsin is a univalent acid with a value for pK of 6.85 (or a base, with pK 7.39).\n\n2. The autodestruction of the pepsin is shown to be dependent in part upon an instantaneous irreversible change occurring in the ionized form of the enzyme (if it be an acid) or in the unionized form (if it be a base). \n\n3. A further progressive autodestruction of pepsin at any given hydrogen ion concentration and temperature is defined by the mass law equation for a monomolecular reaction \n\n4. The velocity of autodestruction of pepsin is directly proportional to the hydroxyl ion concentration. It is much less in the range of hydroxyl ion concentration from pOH 9.89-7.7, than in the range greater than pOH 7.7. In both of these ranges variations in pK with pOH may be represented by straight lines.", "doi": "10.1085/jgp.10.3.451", "pmcid": "PMC2140918", "issn": "0022-1295", "publisher": "Rockefeller University Press", "publication": "Journal of General Physiology", "publication_date": "1927-01-20", "series_number": "3", "volume": "10", "issue": "3", "pages": "451-467" }, { "id": "authors:kshyg-pqy89", "collection": "authors", "collection_id": "kshyg-pqy89", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:MCFjgp27", "type": "article", "title": "The stages of the peptic hydrolysis of egg albumin", "author": [ { "family_name": "McFarlane", "given_name": "Jennie", "clpid": "McFarlane-J" }, { "family_name": "Dunbar", "given_name": "Violet E.", "clpid": "Dunbar-V-E" }, { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Wasteneys", "given_name": "Hardolph", "clpid": "Wasteneys-H" } ], "abstract": "1. Most of the products of the peptic hydrolysis of albumin, about 85 per cent of the total N, are primary in the sense that they arise directly from the protein molecule, and undergo no further hydrolysis. \n\n2. A slow secondary hydrolysis, involving about 15 per cent of the total N, occurs in the proteose and simpler fractions primarily split off. \n\n3. Acid metaprotein in peptic hydrolysis arises as a result of the action of add. It is not an essential stage in the hydrolysis of undenatured albumin. \n\n4. Acid metaprotein is hydrolyzed by pepsin more slowly under comparable conditions than undenatured albumin.", "doi": "10.1085/jgp.10.3.437", "pmcid": "PMC2140919", "issn": "0022-1295", "publisher": "Rockefeller University Press", "publication": "Journal of General Physiology", "publication_date": "1927-01", "series_number": "3", "volume": "10", "issue": "3", "pages": "437-450" }, { "id": "authors:ckewv-j7z44", "collection": "authors", "collection_id": "ckewv-j7z44", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:20140115-114229611", "type": "article", "title": "The Enzymatic Synthesis Of Protein. V. A Note On The Synthesizing Action Of Trypsin", "author": [ { "family_name": "Wasteneys", "given_name": "Hardolph", "clpid": "Wasteneys-H" }, { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" } ], "abstract": "In extending our investigation of the enzymatic synthesis of protein\nto the synthesizing action of commercial trypsin (1) the findings\nof Henriques and Gjaldb\u00e4k (2) were reviewed. In their experiments\non plastein formation by trypsin, these authors observed\na curious simultaneous hydrolysis and synthesis. This observation\nis confirmed.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1925-04-01", "series_number": "3", "volume": "63", "issue": "3", "pages": "575-578" }, { "id": "authors:khpxv-yjn55", "collection": "authors", "collection_id": "khpxv-yjn55", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc25b", "type": "article", "title": "The enzymatic synthesis of protein. IV. The effect of concentration on peptic synthesis", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Wasteneys", "given_name": "Hardolph", "clpid": "Wasteneys-H" } ], "abstract": "In the enzymatic hydrolysis and synthesis of proteins in vitro, the important factor, the factor upon which the direction and the degree of the reaction are dependent, is not the relative concentration of water, but the concentration of material in solution. This conclusion, pointed out by Moore, the authors have discussed at length in a previous paper (1). As shown there, the molecular concentration of water is always so enormously greater than that of the other components that the small amounts added or removed in the course of either reaction are negligible, and it may, therefore, be considered as remaining constant. The distinguishing feature of the hydrolysis and synthesis of protein is the conversion of 1 molecule of protein into a number of molecules of products. It is this characteristic which is responsible for complete hydrolysis in dilute solutions and for the ease with which synthesis is achieved in concentrated solutions. It follows that the extent of synthesis will increase as the concentration increases, and that as the concentration decreases a point will be reached at which synthesis will fail. The concentration at this point will correspond to the maximum concentration of protein capable of complete hydrolysis.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1925-04", "series_number": "3", "volume": "63", "issue": "3", "pages": "563-574" }, { "id": "authors:9x3ez-aee32", "collection": "authors", "collection_id": "9x3ez-aee32", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:BORjbc25a", "type": "article", "title": "The enzymatic synthesis of protein. II. The effect of temperature on the synthesizing action of pepsin", "author": [ { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" }, { "family_name": "Wasteneys", "given_name": "Hardolph", "clpid": "Wasteneys-H" } ], "abstract": "In a solution of the products of the hydrolysis of protein it is theoretically possible to bring about the reverse reaction, i.e. synthesis, in two ways: by concentrating the solution, and by raising the temperature. The theoretical considerations from which the first of these conclusions was deduced have been discussed in a previous paper (1). It is sufficient to recapitulate here, that the first method is predictable from an appropriate statement of the mass law. The experimental confirmation of the prediction was described by the authors (1). The second method is predictable from certain thermodynamical considerations of reversible reactions pointed out by Moore (2). He deduced the equilibrium equation P\u03b1, = K Pnb, where P\u03b1, and Pb, are respectively the osmotic pressures of the substrate and its product, and K is a constant. K is a symbol for the expression P0eC/RT, where P and e are constants, R is the gas constant, C is the chemical energy involved in the breakdown of 1 gram molecule of A into n gram molecules of B, and T is the absolute temperature.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1925-01", "series_number": "3", "volume": "62", "issue": "3", "pages": "633-639" }, { "id": "authors:ark26-y9c66", "collection": "authors", "collection_id": "ark26-y9c66", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:20140902-143116989", "type": "article", "title": "The enzymatic synthesis of protein. III. The effect of the hydrogen ion concentration on peptic synthesis", "author": [ { "family_name": "Wasteneys", "given_name": "Hardolph", "clpid": "Wasteneys-H" }, { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" } ], "abstract": "In two previous communications the authors have described a\nsynthesis of protein by pepsin in a concentrated peptic hydrolysate\nof albumin (1); and the effect of temperature on this synthesis\n(2). The justification for describing the synthetic product as\nprotein is discussed in our previous paper (2). In these communications\nthe optimum hydrogen ion concentration was stated to be\npH 4.0; but the influence of the hydrogen ion concentration was\notherwise not discussed. The importance of the degree of acidity\nwas realized early by Sawjalow (3), who did not, however, define\nit precisely, and by Henriques and Gjaldb\u00e4k (4), who gave the\noptimum pH as 1.5. This hydrogen ion concentration in our\nexperience, despite the existence of all other optimum conditions,\nallows only very small amounts of synthesis. Either Henriques\nand Gjaldb\u00e4k were in error, or the occurrence of the optimum pH\nat 1.5 was due to some as yet unrecognized factor.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1925-01", "series_number": "3", "volume": "62", "issue": "3", "pages": "675-686" }, { "id": "authors:0qyde-zhv33", "collection": "authors", "collection_id": "0qyde-zhv33", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:20140902-141818800", "type": "article", "title": "The enzymatic synthesis of protein. I. The sythesizing action of pepsin", "author": [ { "family_name": "Wasteneys", "given_name": "Hardolph", "clpid": "Wasteneys-H" }, { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" } ], "abstract": "A condition in which a synthesis of protein-like material occurs, was\nfirst arranged in 1886 by Danilewski (1) who observed the formation of a\nprecipitate when stomach extract was added to a concentrated solution\nof the products of peptic hydrolysis. He considered the causative agent\nto be an enzyme, because precipitation did not occur if the stomach extract\nhad been previously heated to 100\u00b0C. This result was confirmed in 1895 by\nOkunew. Both Danilewski and Okunew concluded that the reaction involved\nsynthesis of the products of protein decomposition into a more composite\nmolecule approaching in complexity a native protein.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1924-11", "series_number": "1", "volume": "62", "issue": "1", "pages": "15-29" }, { "id": "authors:h25gm-nt914", "collection": "authors", "collection_id": "h25gm-nt914", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:20140902-141422250", "type": "article", "title": "A method for the fractional analysis of incomplete protein hydrolysates", "author": [ { "family_name": "Wasteneys", "given_name": "Hardolph", "clpid": "Wasteneys-H" }, { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" } ], "abstract": "The constituents of an enzymatic hydrolysate of protein can be\ndivided according to their complexity, into six fractions; protein,\nmetaprotein, proteose, peptone, subpeptones, and amino acids.\nA method for the quantitative estimation of these fractions\nwas devised in order to secure more definite information regarding\nthe changes occurring during hydrolysis than is obtained by the\nusual free amino nitrogen determinations. The method has stood\nthe test of continued use by different workers for over a year, and\nhas given consistently accurate results.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1924-11", "series_number": "1", "volume": "62", "issue": "1", "pages": "1-14" }, { "id": "authors:3dw5p-4hb94", "collection": "authors", "collection_id": "3dw5p-4hb94", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:HUNjbc23", "type": "article", "title": "Nitrogen distribution by globin", "author": [ { "family_name": "Hunter", "given_name": "Andrew", "clpid": "Hunter-A" }, { "family_name": "Borsook", "given_name": "Henry", "clpid": "Borsook-H" } ], "abstract": "This and other experiences with the tryptophane method of F\u00fcrth and Nobel led us to doubt seriously the reliability of quantitative data obtained by its application. When, therefore, just as we completed our work with it, Folin and Looney (6) described another and apparently better method of determination, a method based upon a different color reaction and capable moreover of convenient combination with a quantitative procedure for tyrosine, it seemed to us worth while to review the problem again. With the aid of this newer method we have now determined the tryptophane and tyrosine content of two series of globin preparations, and have, we believe, settled fairly decisively the proportion of these amino-acids yielded by the pure protein. We have also taken occasion to determine by the method of Van Slyke the general distribution of nitrogen in the globin molecule.", "issn": "0021-9258", "publisher": "American Society for Biochemistry and Molecular Biology", "publication": "Journal of Biological Chemistry", "publication_date": "1923-09", "series_number": "2", "volume": "57", "issue": "2", "pages": "507-514" } ]