[ { "id": "https://authors.library.caltech.eduhttps://authors.library.caltech.edu/records/fj4js-5m332", "eprint_id": 955, "eprint_status": "archive", "datestamp": "2023-08-22 04:05:49", "lastmod": "2023-10-13 22:03:26", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Margalit-R", "name": { "family": "Margalit", "given": "Ruth" } }, { "id": "Kosti\u0107-N-M", "name": { "family": "Kosti\u0107", "given": "Nenad M." } }, { "id": "Che-Chi-Ming", "name": { "family": "Che", "given": "Chi-Ming" } }, { "id": "Blair-D-F", "name": { "family": "Blair", "given": "David F." } }, { "id": "Chiang-Huey-Jenn", "name": { "family": "Chiang", "given": "Huey-Jenn" } }, { "id": "Pecht-I", "name": { "family": "Pecht", "given": "Israel" } }, { "id": "Shelton-Joan-B", "name": { "family": "Shelton", "given": "Joan B." } }, { "id": "Shelton-J-Roger", "name": { "family": "Shelton", "given": "J. Roger" } }, { "id": "Schroeder-W-A", "name": { "family": "Schroeder", "given": "Walter A." } }, { "id": "Gray-H-B", "name": { "family": "Gray", "given": "Harry B." }, "orcid": "0000-0002-7937-7876" } ] }, "title": "Preparation and characterization of pentaammineruthenium-(histidine-83)azurin: Thermodynamics of intramolecular electron transfer from ruthenium to copper", "ispublished": "pub", "full_text_status": "public", "keywords": "ruthenium-histidine binding, protein modification, blue copper, oxido-reduction, reorganization energy", "note": "\u00a9 1984 by the National Academy of Sciences. \n\nContributed by Harry B. Gray, May 29, 1984. \n\nWe thank Stephen Mayo for Fig. 3, Vance Morgan for help with the CD measurements, Tin Wu Tang for assistance with cyclic voltammetry, and Ting Lin Kao for a sample of Na[Co(EDTA)]. Helpful comments were provided by Walther Ellis, Karl Freed, Michel Goldberg, Brian Hoffman, John Hopfield, Noel Hush, Sven Larsson, George McLendon, Bo Malmstrom, and Rudy Marcus. This research was supported by National Institutes of Health Grants AM19038 (H.B.G.) and HL02558 (W.A.S.). This is contribution no. 7033 from the Arthur Amos Noyes Laboratory. \n\nThe publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked \"advertisement\" in accordance with 18 U.S.C. \u00a71734 solely to indicate this fact.\n\n
Published - MARpnas84.pdf
", "abstract": "The reaction between a5RuH2O2+ (a is NH3) and Pseudomonas aeruginosa azurin at pH 7, followed by oxidation, yields a5Ru(His-83)3+-azurin(Cu2+) as the major product. Spectroscopic measurements (UV-visible, CD, EPR, and resonance Raman) indicate that the native structure is maintained in the modified protein. The site of ruthenium binding (His-83) was identified by peptide mapping. The a5RuHis/Cu ratio in the modified protein, determined from the EPR spectrum, is 1:1, and the reduction potentials (vs. normal hydrogen electrode, pH 7.0, 25 degrees C) are blue copper (Cu2+/1+), 320 \u00b1 2 mV; a5Ru(His-83)3+/2+, 50 \u00b1 10 mV. From measurements of the reduction potentials at several temperatures in the 5-40 degrees C range, delta-H degrees for intramolecular Ru2+ --> Cu2+ electron transfer was estimated to be -12.4 kcal mol(-1) (1 cal = 4.184 J). Analysis of kinetic data in light of the electron transfer exothermicity indicates that the reorganizational enthalpy of the blue copper site can be no larger than 7.1 kcal mol(-1).", "date": "1984-10-15", "date_type": "published", "publication": "Proceedings of the National Academy of Sciences of the United States of America", "volume": "81", "number": "20", "publisher": "National Academy of Sciences", "pagerange": "6554-6558", "id_number": "CaltechAUTHORS:MARpnas84", "issn": "0027-8424", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:MARpnas84", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "NIH", "grant_number": "AM19038" }, { "agency": "NIH", "grant_number": "HL02558" } ] }, "other_numbering_system": { "items": [ { "id": "7033", "name": "Arthur Amos Noyes Laboratory of Chemical Physics" } ] }, "doi": "10.1073/pnas.81.20.6554", "pmcid": "PMC391964", "primary_object": { "basename": "MARpnas84.pdf", "url": "https://authors.library.caltech.edu/records/fj4js-5m332/files/MARpnas84.pdf" }, "resource_type": "article", "pub_year": "1984", "author_list": "Margalit, Ruth; Kosti\u0107, Nenad M.; et el." }, { "id": "https://authors.library.caltech.eduhttps://authors.library.caltech.edu/records/zqzkc-h8373", "eprint_id": 6878, "eprint_status": "archive", "datestamp": "2023-08-22 03:53:00", "lastmod": "2023-10-16 20:35:15", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "DeSimone-J", "name": { "family": "DeSimone", "given": "Joseph" } }, { "id": "Schroeder-W-A", "name": { "family": "Schroeder", "given": "W. A." } }, { "id": "Shelton-Joan-B", "name": { "family": "Shelton", "given": "Joan B." } }, { "id": "Shelton-J-Roger", "name": { "family": "Shelton", "given": "J. Roger" } }, { "id": "Espinueva-Z", "name": { "family": "Espinueva", "given": "Zenaida" } }, { "id": "Huynh-Van", "name": { "family": "Huynh", "given": "Van" } }, { "id": "Hall-Lemuel", "name": { "family": "Hall", "given": "Lemuel" } }, { "id": "Zwiers-D", "name": { "family": "Zwiers", "given": "David" } } ] }, "title": "Speciation in the baboon and its relation to gamma-chain heterogeneity and to the response to induction of HbF by 5-azacytidine", "ispublished": "pub", "full_text_status": "public", "note": "\u00a9 1984 by The American Society of Hematology \n\nSubmitted August 4, 1983; accepted November 14, 1983. \n\nSupported in part by Grants HL-20920 and HL-02558 from the National Institutes of Health, and Veterans Administration Senior Medical Investigator Research funds. \n\nDivision of Chemistry and Chemical Engineering (Contribution no. 6870), California Institute of Technology, Pasadena, CA.\n\nPublished - DESblo84.pdf
", "abstract": "In the baboon (Papio species), the two nonallelic gamma-genes produce gamma-chains that differ at a minimum at residue 75, where isoleucine (I gamma-chain) or valine (V gamma) may be present. This situation obtains in baboons that are sometimes designated as Papio anubis, Papio hamadryas, and Papio papio. However, in Papio cynocephalus, although the I gamma-chains are identical with those in the above mentioned types, the V gamma-chains have the substitutions ala----gly at residue 9 and ala----val at residue 23. The V gamma-chains of P. cynocephalus are called V gamma C to distinguish them from the V gamma A-chains of P. anubis, etc. A single cynocephalus animal has been found to have only normal I gamma-chains and I gamma C-chains (that is, glycine in residue 9, valine in 23, and isoleucine in 75). When HbF is produced in response to stress with 5-azacytidine, P. anubis baboons respond with greater production than do P. cynocephalus, and hybrids fall between. Minimal data on P. hamadryas and P. papio suggest an even lower response than P. cynocephalus. As HbF increases under stress, the ratio of I gamma to V gamma-chains changes from the value in the adult or juvenile baboon toward the ratio in the newborn baboon. However, it does not attain the newborn value. The V gamma A and V gamma C-genes respond differently to stress. In hybrids, the production of V gamma A- chains exceeds that of V gamma C-chains. A controlling factor in cis apparently is present and may be responsible for the species-related extent of total HbF production. It may be concluded that the more primitive the cell in the erythroid maturation series that has been subjected to 5-azacytidine, the more active is the I gamma-gene.", "date": "1984-05", "date_type": "published", "publication": "Blood", "volume": "63", "number": "5", "publisher": "American Society of Hematology", "pagerange": "1088-1095", "id_number": "CaltechAUTHORS:DESblo84", "issn": "0006-4971", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:DESblo84", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "NIH", "grant_number": "HL-20920" }, { "agency": "NIH", "grant_number": "HL-02558" }, { "agency": "Veterans Administration" } ] }, "other_numbering_system": { "items": [ { "id": "6870", "name": "Caltech Division of Chemistry and Chemical Engineering" } ] }, "doi": "10.1182/blood.V63.5.1088.1088", "primary_object": { "basename": "DESblo84.pdf", "url": "https://authors.library.caltech.edu/records/zqzkc-h8373/files/DESblo84.pdf" }, "resource_type": "article", "pub_year": "1984", "author_list": "DeSimone, Joseph; Schroeder, W. A.; et el." }, { "id": "https://authors.library.caltech.eduhttps://authors.library.caltech.edu/records/eddr4-5ap15", "eprint_id": 1010, "eprint_status": "archive", "datestamp": "2023-08-22 03:15:16", "lastmod": "2023-10-13 22:04:46", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Yocom-K-M", "name": { "family": "Yocom", "given": "Kathryn M." } }, { "id": "Shelton-Joan-B", "name": { "family": "Shelton", "given": "Joan B." } }, { "id": "Shelton-J-Roger", "name": { "family": "Shelton", "given": "J. Roger" } }, { "id": "Schroeder-W-A", "name": { "family": "Schroeder", "given": "Walter A." } }, { "id": "Worosila-G", "name": { "family": "Worosila", "given": "Greg" } }, { "id": "Isied-S-S", "name": { "family": "Isied", "given": "Stephan S." } }, { "id": "Bordignon-E", "name": { "family": "Bordignon", "given": "Emilio" } }, { "id": "Gray-H-B", "name": { "family": "Gray", "given": "Harry B." }, "orcid": "0000-0002-7937-7876" } ] }, "title": "Preparation and characterization of a pentaammineruthenium(III) derivative of horse heart ferricytochrome c", "ispublished": "pub", "full_text_status": "public", "keywords": "ruthenium-histidine binding, modified cytochromes, electrochemistry", "note": "\u00a9 1982 by the National Academy of Sciences. \n\nContributed by Harry B. Gray, August 23, 1982. \n\nOur research on cytochrome c derivatives has been aided greatly by numerous discussions with Dick Dickerson, Walther Ellis, John Hopfield, Bo Malmstrom, Rudy Marcus, Chuck Root, Norman Sutin, Henry Taube, and Henrique Toma. NMR spectra were obtained at the Stanford University NMR Laboratory (supported by National Science Foundation Grant GP23633 and National Institutes of Health Grant RR 00711). Research at California Institute of Technology was supported by National Science Foundation Grant CHE80-24863 (K.M.Y., E.B., and H.B.G.) and by National Institutes of Health Grant HL 02558 (J.B.S., J.R.S., and W.A.S.). Research at Rutgers University was supported by National Institutes of Health Grant GM 26324 (S.S.1.). S.S.I. acknowledges a National Institutes of Health Career Development Award (AM 00734) (1980-1985) and a Camille and Henry Dreyfus Teacher-Scholar Award. This is contribution no. 6706 from the Arthur Amos Noyes Laboratory. \n\nThe publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked \"advertisement\" in accordance with 18 U. S. C. \u00a71734 solely to indicate this fact.\n\nPublished - YOCpnas82.pdf
", "abstract": "A stable complex between pentaammineruthenium(III) and histidine-33 in horse heart ferricytochrome c is formed in the reaction between aquopentaammineruthenium(II) and the protein at pH 7. HPLC of the tryptic hydrolysate of the modified protein was employed to identify the pentaammineruthenium binding site. Spectroscopic measurements show that the integrity of the native structure in the vicinity of the heme c group is maintained in the ruthenium-modified protein. The reduction potentials are: heme c (Fe3+/2+), 0.26 V; Ru(NH3)5(His-33)3+/2+, 0.15 V (vs. normal hydrogen electrode).", "date": "1982-11-15", "date_type": "published", "publication": "Proceedings of the National Academy of Sciences of the United States of America", "volume": "79", "number": "22", "publisher": "National Academy of Sciences", "pagerange": "7052-7055", "id_number": "CaltechAUTHORS:YOCpnas82", "issn": "0027-8424", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:YOCpnas82", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "NSF", "grant_number": "GP23633" }, { "agency": "NIH", "grant_number": "RR 00711" }, { "agency": "NSF", "grant_number": "CHE80-24863" }, { "agency": "NIH", "grant_number": "HL02558" }, { "agency": "NIH", "grant_number": "GM26324" }, { "agency": "NIH", "grant_number": "AM00734" }, { "agency": "Camille and Henry Dreyfus Foundation" } ] }, "other_numbering_system": { "items": [ { "id": "6706", "name": "Arthur Amos Noyes Laboratory of Chemical Physics" } ] }, "doi": "10.1073/pnas.79.22.7052", "pmcid": "PMC347273", "primary_object": { "basename": "YOCpnas82.pdf", "url": "https://authors.library.caltech.edu/records/eddr4-5ap15/files/YOCpnas82.pdf" }, "resource_type": "article", "pub_year": "1982", "author_list": "Yocom, Kathryn M.; Shelton, Joan B.; et el." }, { "id": "https://authors.library.caltech.eduhttps://authors.library.caltech.edu/records/xwmnb-wn312", "eprint_id": 106868, "eprint_status": "archive", "datestamp": "2023-08-22 01:36:00", "lastmod": "2023-10-23 15:07:56", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Ringelhann-B", "name": { "family": "Ringelhann", "given": "B." } }, { "id": "Acquaye-C-T-A", "name": { "family": "Acquaye", "given": "C. T. A." } }, { "id": "Oldham-J-H", "name": { "family": "Oldham", "given": "J. H." } }, { "id": "Konotey-Ahulu-F-I-D", "name": { "family": "Konotey-Ahulu", "given": "F. I. D." } }, { "id": "Yawson-G", "name": { "family": "Yawson", "given": "G." } }, { "id": "Sukumaran-P-K", "name": { "family": "Sukumaran", "given": "P. K." } }, { "id": "Schroeder-W-A", "name": { "family": "Schroeder", "given": "W. A." } }, { "id": "Huisman-T-H-J", "name": { "family": "Huisman", "given": "T. H. J." } } ] }, "title": "Homozygotes for the hereditary persistence of fetal hemoglobin: The ratio of ^G\u03b3 to ^A\u03b3 chains and biosynthetic studies", "ispublished": "pub", "full_text_status": "public", "keywords": "HPFH homozgote; \u03b3-chain type; globin chain synthesis", "note": "\u00a9 1977 Springer. \n\nReceived 20 January 1977; Accepted 25 April 1977.", "abstract": "Two sons of a previously reported Ghanaian homozygote for the hereditary persistence of fetal hemoglobin (HPFH) (Ringelhann et al., 1970) also are HPFH homozygotes. In addition, another unrelated adult Ghanaian homozygote has been detected. All of these Ghanaian homozygotes as well as three American Black HPFH homozygotes have the ^G\u03b3^A\u03b3 type of HPFH with a ^G\u03b3 to ^A\u03b3 ratio of about 3:2, in contrast to an Asiatic Indian homozygote who has the ^G\u03b3 type. Globin chain synthesis in HPFH homozygotes is unbalanced, with a \u03b3/\u03b1 ratio of 0.6 or less, whereas it is balanced in heterozygotes according to most reports.", "date": "1977-12", "date_type": "published", "publication": "Biochemical Genetics", "volume": "15", "number": "11-12", "publisher": "Springer", "pagerange": "1083-1096", "id_number": "CaltechAUTHORS:20201201-130559876", "issn": "0006-2928", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:20201201-130559876", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "doi": "10.1007/bf00484499", "resource_type": "article", "pub_year": "1977", "author_list": "Ringelhann, B.; Acquaye, C. T. A.; et el." }, { "id": "https://authors.library.caltech.eduhttps://authors.library.caltech.edu/records/7hvmr-3cn80", "eprint_id": 117245, "eprint_status": "archive", "datestamp": "2023-08-22 01:31:23", "lastmod": "2023-10-24 22:27:32", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Huisman-T-H-J", "name": { "family": "Huisman", "given": "T. H. J." } }, { "id": "Harris-H", "name": { "family": "Harris", "given": "H." } }, { "id": "Gravely-M", "name": { "family": "Gravely", "given": "M." } }, { "id": "Schroeder-W-A", "name": { "family": "Schroeder", "given": "W. A." } }, { "id": "Shelton-J-R", "name": { "family": "Shelton", "given": "J. R." } }, { "id": "Shelton-J-B", "name": { "family": "Shelton", "given": "J. B." } }, { "id": "Evans-L", "name": { "family": "Evans", "given": "L." } } ] }, "title": "The chemical heterogeneity of the fetal hemoglobin in normal newborn infants and in adults", "ispublished": "pub", "full_text_status": "public", "keywords": "Cell Biology; Clinical Biochemistry; Molecular Biology; General Medicine", "note": "An invited article.\nContribution No. 5499.", "date": "1977-08", "date_type": "published", "publication": "Molecular and cellular biochemistry", "volume": "17", "number": "1", "publisher": "Springer", "pagerange": "45-55", "id_number": "CaltechAUTHORS:20221004-680171300.22", "issn": "0300-8177", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:20221004-680171300.22", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "other_numbering_system": { "items": [ { "id": "5499", "name": "Contribution" } ] }, "doi": "10.1007/bf01732554", "resource_type": "article", "pub_year": "1977", "author_list": "Huisman, T. H. J.; Harris, H.; et el." }, { "id": "https://authors.library.caltech.eduhttps://authors.library.caltech.edu/records/xqpep-v1q60", "eprint_id": 10565, "eprint_status": "archive", "datestamp": "2023-08-21 23:42:49", "lastmod": "2023-10-16 22:56:29", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Schroeder-W-A", "name": { "family": "Schroeder", "given": "W. A." } }, { "id": "Huisman-T-H-J", "name": { "family": "Huisman", "given": "T. H. J." } }, { "id": "Shelton-J-Roger", "name": { "family": "Shelton", "given": "J. Roger" } }, { "id": "Shelton-Joan-B", "name": { "family": "Shelton", "given": "Joan Balog" } }, { "id": "Kleihauer-E-F", "name": { "family": "Kleihauer", "given": "Enno F." } }, { "id": "Dozy-A-M", "name": { "family": "Dozy", "given": "Andr\u00e9e M." } }, { "id": "Robberson-Barbara", "name": { "family": "Robberson", "given": "Barbara" } } ] }, "title": "Evidence for multiple structural genes for the \u03b3 chain of human fetal hemoglobin", "ispublished": "pub", "full_text_status": "public", "note": "\u00a9 1968 by the National Academy of Sciences. \n\nCommunicated by Ray D. Owen, April 5, 1968. \n\nWe appreciate the helpful discussions on genetics with Drs. E.B. Lewis and Ray D. Owen. Dr. Audrey Brown (Department of Pediatrics, Medical College of Georgia) assisted us in obtaining additional samples from babies D.P., W.B., and C.W. We are also indebted to Dr. Edgar Ahern (Department of Pathology, University College Hospital, Jamaica, W.I.) who made samples from baby J. B. available to us. Mr. Gerald Apell assisted in some of the experimental work. This investigation was supported in part by grants (HE-02558 and HE-05168) from the National Institutes of Health, U.S. Public Health Service. E.F.K. was supported by USPHS grant 1 FOS-TW-1127-01 as an International Research Fellow on leave from the Department of Pediatrics, University of Munich, Germany. \n\nDivision of Chemistry and Chemical Engineering, Contribution no. 3668.\n\nPublished - SCHRpnas68.pdf
", "abstract": "A sequence with a specific residue at each position was proposed for the \u03b3 chain of human fetal hemoglobin by Schroeder et al. (1) after a study in which hemoglobin from a number of individual infants was used. We have now examined in part the fetal hemoglobin components of 17 additional infants and have observed that position 136 of the \u03b3 chain may be occupied not only by a glycyl residue, as previously reported, but also by an alanyl residue.", "date": "1968-06", "date_type": "published", "publication": "Proceedings of the National Academy of Sciences of the United States of America", "volume": "60", "number": "2", "publisher": "National Academy of Sciences", "pagerange": "537-544", "id_number": "CaltechAUTHORS:SCHRpnas68", "issn": "0027-8424", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:SCHRpnas68", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "NIH", "grant_number": "HE-02558" }, { "agency": "NIH", "grant_number": "HE-05168" }, { "agency": "NIH Postdoctoral Fellowship", "grant_number": "1 FOS-TW-1127-01" } ] }, "doi": "10.1073/pnas.60.2.537", "pmcid": "PMC225081", "primary_object": { "basename": "SCHRpnas68.pdf", "url": "https://authors.library.caltech.edu/records/xqpep-v1q60/files/SCHRpnas68.pdf" }, "resource_type": "article", "pub_year": "1968", "author_list": "Schroeder, W. A.; Huisman, T. H. J.; et el." }, { "id": "https://authors.library.caltech.eduhttps://authors.library.caltech.edu/records/c2d2m-hjz44", "eprint_id": 91061, "eprint_status": "archive", "datestamp": "2023-08-19 04:31:19", "lastmod": "2023-10-19 22:06:13", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Jones-R-T", "name": { "family": "Jones", "given": "Richard T." } }, { "id": "Schroeder-W-A", "name": { "family": "Schroeder", "given": "W. A." } } ] }, "title": "Chemical Characterization and Subunit Hybridization of Human Hemoglobin H and Associated Compounds", "ispublished": "pub", "full_text_status": "public", "note": "\u00a9 1963 American Chemical Society. \n\nReceived April 1, 1963. \n\nThe authors wish to thank Drs. D. A. Rigas, R. D. Koler, P. Sturgeon, and W. R. Bergren for obtaining samples of blood and for their valuable help and discussions during the course of this work. A sample of hemoglobin Bart's was obtained from Dr. H. Lehmann. Mrs. Joan Balog Shelton carried out the determinations of the N-terminal sequences. Special thanks are due to Dr. J. R. Vinograd for the gift of some radioactive hemoglobins, for assistance in the preparation of other samples, for supervising the determination of sedimentation constants which was done with the aid of Mrs. Janet Morris, and for valuable discussions. \n\nThis investigation has been supported in part by a grant (H-2558) from the National Institutes of Health, United States Public Health Service, through the use of equipment and chemicals that had been purchased under the grant. \n\nNational Research Fellow in the Medical Sciences, 1958, and Postdoctoral Fellow of the Heart Institute, United States Public Health Service, 1960.\n\nPublished - bi00906a031.pdf
", "abstract": "Two abnormal hemoglobin components have been detected in association with thalassemiahemoglobin H disease. These components, as well as the major hemoglobin component, have been chemically characterized by determination of the amino acid composition, N-terminal amino acid sequence, tryptic peptide patterns, sedimentation coefficients, and subunit hybridization. The abnormal component in larger amount has a subunit formula of \u03b2_4; the abnormal component in smaller amount has a subunit formula of \u03b3_4. The major hemoglobin component could not be distinguished chemically from normal hemoglobin A. Subunit hybridization studies of hemoglobins indicate that the affinities of the various subunits for one another are not equal.", "date": "1963-11", "date_type": "published", "publication": "Biochemistry", "volume": "2", "number": "6", "publisher": "American Chemical Society", "pagerange": "1357-1367", "id_number": "CaltechAUTHORS:20181119-161053942", "issn": "0006-2960", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:20181119-161053942", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "NIH", "grant_number": "H-2558" }, { "agency": "National Research Fellow in the Medical Sciences" }, { "agency": "NIH Postdoctoral Fellowship" } ] }, "other_numbering_system": { "items": [ { "id": "2961", "name": "Division of Chemistry and Chemical Engineering" } ] }, "doi": "10.1021/bi00906a031", "primary_object": { "basename": "bi00906a031.pdf", "url": "https://authors.library.caltech.edu/records/c2d2m-hjz44/files/bi00906a031.pdf" }, "resource_type": "article", "pub_year": "1963", "author_list": "Jones, Richard T. and Schroeder, W. A." }, { "id": "https://authors.library.caltech.eduhttps://authors.library.caltech.edu/records/ad6je-wsg94", "eprint_id": 91060, "eprint_status": "archive", "datestamp": "2023-08-19 04:27:57", "lastmod": "2023-10-19 22:06:10", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Schroeder-W-A", "name": { "family": "Schroeder", "given": "W. A." } }, { "id": "Shelton-J-Roger", "name": { "family": "Shelton", "given": "J. Roger" } }, { "id": "Shelton-Joan-B", "name": { "family": "Shelton", "given": "Joan Balog" } }, { "id": "Cormick-Jean", "name": { "family": "Cormick", "given": "Jean" } }, { "id": "Jones-Richard-T", "name": { "family": "Jones", "given": "Richard T." } } ] }, "title": "The Amino Acid Sequence of the \u03b3 Chain of Human Fetal Hemoglobin", "ispublished": "pub", "full_text_status": "restricted", "note": "\u00a9 1963 American Chemical Society. \n\nReceived April 15, 1963. \n\nWe wish to express our thanks to Dr. D. Armstrong, Dr. M. Lazarus, and Dr. T. Perry through whom some samples of cord blood were obtained. Mr. J. T. Cua and Mr. W. D. Fenninger rendered capable assistance in some of the experiments. \n\nThis investigation was supported in part by a grant (H-2558) from the National Institutes of Health, United States Public Health Service.", "abstract": "The 146 amino acid residues of the \u03b3 chain of human fetal hemoglobin have been placed in sequence. The fetal hemoglobin for this investigation was isolated chromatographically from umbilical cord blood. The \u03b1 and \u03b3 chains were separated prior to the determination of sequence. For the determination of the sequence, peptides were produced by individual hydrolyses with trypsin, chymotrypsin, or pepsin. The sequence of the individual peptides was determined largely through the application of the Edman degradation. The differences between the \u03b3 chains of human fetal hemoglobin and the \u03b2 chains of human adult hemoglobin are responsible for the differences in the properties of the two molecules.", "date": "1963-09", "date_type": "published", "publication": "Biochemistry", "volume": "2", "number": "5", "publisher": "American Chemical Society", "pagerange": "992-1008", "id_number": "CaltechAUTHORS:20181119-161053839", "issn": "0006-2960", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:20181119-161053839", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "NIH", "grant_number": "H-2558" } ] }, "other_numbering_system": { "items": [ { "id": "2996", "name": "Caltech Division of Chemistry and Chemical Engineering" } ] }, "doi": "10.1021/bi00905a016", "resource_type": "article", "pub_year": "1963", "author_list": "Schroeder, W. A.; Shelton, J. Roger; et el." }, { "id": "https://authors.library.caltech.eduhttps://authors.library.caltech.edu/records/2bypt-a2r28", "eprint_id": 91059, "eprint_status": "archive", "datestamp": "2023-08-19 04:13:09", "lastmod": "2023-10-19 22:06:03", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Schroeder-W-A", "name": { "family": "Schroeder", "given": "W. A." } }, { "id": "Jones-R-T", "name": { "family": "Jones", "given": "Richard T." } }, { "id": "Cromick-J", "name": { "family": "Cromick", "given": "Jean" } }, { "id": "McCalla-K", "name": { "family": "McCalla", "given": "Kathleen" } } ] }, "title": "Chromatographic Separation of Peptides on Ion Exchange Resins. Separation of Peptides from Enzymatic Hydrolyzates of the \u03b1, \u03b2, and \u03b3 Chains of Human Hemoglobins", "ispublished": "pub", "full_text_status": "restricted", "note": "\u00a9 1962 American Chemical Society. \n\nReceived for review June 11, 1962. Accepted August 30, 1962. \n\nParts of this investigation have had the assistance of J. Roger Shelton and William Fenninger. The composition and use of the pyridine-acetic acid developers on Dowex-50 were suggested by Joe R. Kimmel of the University of Utah. \n\nPresented in part at the 141st meeting of the American Chemical Society, Washington, D. C., March 1962, at the symposium honoring L. Zechmeister as recipient of the ACS Award in Chromatography and Electrophoresis. This investigation has been supported in part by a grant (H-2558) from the National Institutes of Health, United States Public Health Service.", "abstract": "Isolation of components in a mixture is most effectively accomplished by great alteration of conditions from step to step in the separation. This principle has been applied to the separation of complex mixtures of peptides in protein hydrolyzates. Excellent results have been obtained by chromatographing first on the cation exchanger Dowex-50 and then rechromatographing on the anion exchanger Dowex-1. Volatile developers were employed throughout. Experimental procedures are presented, and results are given of their application to the separation of peptides from human hemoglobins A and F.", "date": "1962-11", "date_type": "published", "publication": "Analytical Chemistry", "volume": "34", "number": "12", "publisher": "American Chemical Society", "pagerange": "1570-1575", "id_number": "CaltechAUTHORS:20181119-161053738", "issn": "0003-2700", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:20181119-161053738", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "NIH", "grant_number": "H-2558" } ] }, "other_numbering_system": { "items": [ { "id": "2857", "name": "Division of Chemistry and Chemical Engineering" } ] }, "doi": "10.1021/ac60192a018", "resource_type": "article", "pub_year": "1962", "author_list": "Schroeder, W. A.; Jones, Richard T.; et el." }, { "id": "https://authors.library.caltech.eduhttps://authors.library.caltech.edu/records/b7fft-0dv51", "eprint_id": 91058, "eprint_status": "archive", "datestamp": "2023-08-19 03:46:49", "lastmod": "2023-10-19 22:06:01", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Schnek-A-G", "name": { "family": "Schnek", "given": "A. G." } }, { "id": "Schroeder-W-A", "name": { "family": "Schroeder", "given": "W. A." } } ] }, "title": "The Relation between the Minor Components of Whole Normal Human Adult Hemoglobin as Isolated by Chromatography and Starch Block Electrophoresis", "ispublished": "pub", "full_text_status": "restricted", "note": "\u00a9 1961 American Chemical Society. \n\nReceived June 13, 1960. \n\nIt is a pleasure to acknowledge the benefit of discussions with Dr. Richard T. Jones during the course of this study. Mrs. Jean Cormick and Mrs. Kathleen McCalla assisted in some of the experiments.", "abstract": "Three hemoglobin components may be separated from hemolysates of normal adult red blood cells by starch block electrophoresis: the main component, A_1, moves at a position intermediate between the most slowly moving component, A_2, and the most rapidly moving component, A_3. By chromatography, eight hemoglobin components may be detected: five (A_(Ia), A_(Ib), A_(Ic), A_(Id) and A_(Ie)) move down the column more rapidly than the main component (An) and two move more slowly\n(Ania and Amb). Non-heme containing proteins are also present. The present investigation has determined the correspondence\nbetween the components as isolated by the two methods: A_I contains A_I(c), A_(Id) and A_(Ie), and A_(II); A_2 contains\nA_(IIIb) and non-heme protein(s); A_3 contains A_(Ia), A(Ib) and non-heme protein(s).", "date": "1961-03-20", "date_type": "published", "publication": "Journal of the American Chemical Society", "volume": "83", "number": "6", "publisher": "American Chemical Society", "pagerange": "1472-1478", "id_number": "CaltechAUTHORS:20181119-161053652", "issn": "0002-7863", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:20181119-161053652", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "other_numbering_system": { "items": [ { "id": "2579", "name": "Division of Chemistry and Chemical Engineering" } ] }, "doi": "10.1021/ja01467a046", "resource_type": "article", "pub_year": "1961", "author_list": "Schnek, A. G. and Schroeder, W. A." }, { "id": "https://authors.library.caltech.eduhttps://authors.library.caltech.edu/records/192m1-0z917", "eprint_id": 91057, "eprint_status": "archive", "datestamp": "2023-08-19 03:32:17", "lastmod": "2023-10-19 22:05:55", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Shelton-J-Roger", "name": { "family": "Shelton", "given": "J. Roger" } }, { "id": "Schroeder-W-A", "name": { "family": "Schroeder", "given": "W. A." } } ] }, "title": "Further N-Terminal Sequences in Human Hemoglobins A, S and F by Edman's Phenylthiohydantoin Method", "ispublished": "pub", "full_text_status": "restricted", "note": "\u00a9 1960 American Chemical Society. \n\nReceived January 4, 1960. \n\nWe wish to thank Joan E. Balog for her work in separating the polypeptide chains of hemoglobin and Dr. G. Matsuda and Dr. R. T. Jones for procurement and preparation of hemoglobin solutions. This investigation was supported in part by a grant (H-2258) from the National Institutes of Health, United States Public Health Service.", "abstract": "By means of the Edman phenylthiohydantoin method, the N-terminal sequences in the peptide chains of several human hemoglobins have been found to be as follows: \u03b1^A and \u03b1^F, val-leu-ser-pro-ala-aspNH_2-; \u03b2^A, val-his-leu-thr-pro-glu-; \u03b2^S, val-his-leu-thr-pro-val-; and \u03b3^F, gly-his-phe.", "date": "1960-07-05", "date_type": "published", "publication": "Journal of the American Chemical Society", "volume": "82", "number": "13", "publisher": "American Chemical Society", "pagerange": "3342-3345", "id_number": "CaltechAUTHORS:20181119-161053564", "issn": "0002-7863", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:20181119-161053564", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "NIH", "grant_number": "H-2258" } ] }, "other_numbering_system": { "items": [ { "id": "2508", "name": "Division of Chemistry and Chemical Engineering" } ] }, "doi": "10.1021/ja01498a028", "resource_type": "article", "pub_year": "1960", "author_list": "Shelton, J. Roger and Schroeder, W. A." }, { "id": "https://authors.library.caltech.eduhttps://authors.library.caltech.edu/records/4t4aw-9z689", "eprint_id": 88266, "eprint_status": "archive", "datestamp": "2023-08-19 02:59:59", "lastmod": "2023-10-18 21:55:38", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Rhinesmith-H-S", "name": { "family": "Rhinesmith", "given": "Herbert S." } }, { "id": "Schroeder-W-A", "name": { "family": "Schroeder", "given": "W. A." } }, { "id": "Pauling-L", "name": { "family": "Pauling", "given": "Linus" } } ] }, "title": "A Quantitative Study of the Hydrolysis of Human Dinitrophenyl(DNP)globin: The Number and Kind of Polypeptide Chains in Normal Adult Human Hemoglobin", "ispublished": "pub", "full_text_status": "restricted", "note": "\u00a9 1957 American Chemical Society. \n\nReceived April 11, 1957. \n\nThis investigation was supported in part by a grant from the Ford Foundation and in part by a research grant (RG-4276(C)) from the National Institutes of Health, Public Health Service.", "abstract": "A quantitative investigation of the partial hydrolysis of DNP-globin in refluxing 6 N hydrochloric acid has led to an explanation of our earlier conclusion that normal adult human hemoglobin contains a non-integral number, 3.6, of N-terminal valyl residues per molecule. It is now concluded that 4 E-terminal residues are present. Moreover, it has been found that the molecule contains two kinds of polypeptide chains, with respect to the K-termini. Under the above hydrolytic conditions the N-terminal valyl residues are released as DNP-Val-leu almost quantitatively from two chains (A chains) within 15 min. On continued hydrolysis the other two chains (B chains) release DNP-valine. No N-terminal peptides originating from the B chains have been definitely identified.", "date": "1957-09-11", "date_type": "published", "publication": "Journal of the American Chemical Society", "volume": "79", "number": "17", "publisher": "American Chemical Society", "pagerange": "4682-4686", "id_number": "CaltechAUTHORS:20180725-111211357", "issn": "0002-7863", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:20180725-111211357", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "Ford Foundation" }, { "agency": "NIH", "grant_number": "RG-4276(C)" } ] }, "other_numbering_system": { "items": [ { "id": "2199", "name": "Gates and Crellin Laboratories of Chemistry" } ] }, "doi": "10.1021/ja01574a028", "resource_type": "article", "pub_year": "1957", "author_list": "Rhinesmith, Herbert S.; Schroeder, W. A.; et el." }, { "id": "https://authors.library.caltech.eduhttps://authors.library.caltech.edu/records/mc2bt-49c16", "eprint_id": 88265, "eprint_status": "archive", "datestamp": "2023-08-19 02:54:06", "lastmod": "2023-10-18 21:55:34", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Rhinesmith-H-S", "name": { "family": "Rhinesmith", "given": "Herbert S." } }, { "id": "Schroeder-W-A", "name": { "family": "Schroeder", "given": "W. A." } }, { "id": "Pauling-L", "name": { "family": "Pauling", "given": "Linus" } } ] }, "title": "The N-Terminal Amino Acid Residues of Normal Adult Human Hemoglobin: A Quantitative Study of Certain Aspects of Sanger's DNP-Method", "ispublished": "pub", "full_text_status": "restricted", "note": "\u00a9 1957 American Chemical Society. \n\nReceived August 3, 1956. \n\nWe wish to express our appreciation to Dr. M. Murayama for supplying several samples of hemoglobin and for carrying out the electrophoretic tests for homogeneity, and to Drs. R. Srinivasan and J. Vinograd for making available their unpublished work on the molecular weight of human hemoglobin. This investigation was supported in part by a research grant (RG-4276) from the National Institutes of Health, Public Health Service.", "abstract": "A quantitative redetermination of the N-terminal valyl residues of normal adult human hemoglobin by the DNP-method of Sanger has led us to question the validity of results previously reported. Our experimental results indicate that there are 3,6 N-terminal valyl residues per molecule, based on a molecular weight of 66,700 for human hemoglobin. The essential difference between this value and those of other investigators lies in a correction factor for operational, chromatographic and hydrolytic losses (13%) which is appreciably lower than any previously reported value. This low value is justified by a detailed study of losses with DNP-valine and two peptides, DNP-Val-gly and DNP-Val-leu, the latter an important hydrolytic product of human hemoglobin itself. On the basis of these results an integral value for the number of end groups in human hemoglobin can be achieved only by revising the molecular weight, If, on the other hand, the number of N-terminal valyl residues in human hemoglobin is non-integral, it may well indicate that normal adult human hemoglobin contains more than one kind of molecule.", "date": "1957-02-12", "date_type": "published", "publication": "Journal of the American Chemical Society", "volume": "79", "number": "3", "publisher": "American Chemical Society", "pagerange": "609-615", "id_number": "CaltechAUTHORS:20180725-111211261", "issn": "0002-7863", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:20180725-111211261", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "NIH", "grant_number": "RG-4276" } ] }, "other_numbering_system": { "items": [ { "id": "2118", "name": "Gates and Crellin Laboratories of Chemistry" } ] }, "doi": "10.1021/ja01560a028", "resource_type": "article", "pub_year": "1957", "author_list": "Rhinesmith, Herbert S.; Schroeder, W. A.; et el." }, { "id": "https://authors.library.caltech.eduhttps://authors.library.caltech.edu/records/3rqct-m0369", "eprint_id": 91111, "eprint_status": "archive", "datestamp": "2023-08-19 02:15:15", "lastmod": "2023-10-19 22:10:06", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Schroeder-W-A", "name": { "family": "Schroeder", "given": "W. A." } }, { "id": "LeGette-J", "name": { "family": "LeGette", "given": "Joann" } } ] }, "title": "A Study of the Quantitative Dinitrophenylation of Amino Acids and Peptides", "ispublished": "pub", "full_text_status": "restricted", "note": "\u00a9 1953 American Chemical Society. \n\nReceived May 14, 1953. \n\nThis investigation was supported in part by a grant from the Lederle Laboratories.", "abstract": "[no abstract]", "date": "1953-09-20", "date_type": "published", "publication": "Journal of the American Chemical Society", "volume": "75", "number": "18", "publisher": "American Chemical Society", "pagerange": "4612-4615", "id_number": "CaltechAUTHORS:20181120-153101208", "issn": "0002-7863", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:20181120-153101208", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "Lederle Laboratories" } ] }, "other_numbering_system": { "items": [ { "id": "1807", "name": "Gates and Crellin Laboratories of Chemistry" } ] }, "doi": "10.1021/ja01114a531", "resource_type": "article", "pub_year": "1953", "author_list": "Schroeder, W. A. and LeGette, Joann" }, { "id": "https://authors.library.caltech.eduhttps://authors.library.caltech.edu/records/t993s-8k138", "eprint_id": 91110, "eprint_status": "archive", "datestamp": "2023-08-19 02:15:07", "lastmod": "2023-10-19 22:10:03", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Schroeder-W-A", "name": { "family": "Schroeder", "given": "W. A." } }, { "id": "Honnen-L-R", "name": { "family": "Honnen", "given": "Lewis R." } } ] }, "title": "Correlation between the Structure of Some Dinitrophenyl Peptides and their Chromatographic Behavior on Silicic Acid\u2014Celite", "ispublished": "pub", "full_text_status": "restricted", "note": "\u00a9 1953 American Chemical Society. \n\nReceived May 14, 1953. \n\nWe wish to thank Miss Lois M. Kay and Dr. F. Charlotte Green for having determined the chromatographic properties of some of the DNP-peptides.", "abstract": "[no abstract]", "date": "1953-09-20", "date_type": "published", "publication": "Journal of the American Chemical Society", "volume": "75", "number": "18", "publisher": "American Chemical Society", "pagerange": "4615-4619", "id_number": "CaltechAUTHORS:20181120-153101121", "issn": "0002-7863", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:20181120-153101121", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "other_numbering_system": { "items": [ { "id": "1808", "name": "Gates and Crellin Laboratories of Chemistry" } ] }, "doi": "10.1021/ja01114a532", "resource_type": "article", "pub_year": "1953", "author_list": "Schroeder, W. A. and Honnen, Lewis R." }, { "id": "https://authors.library.caltech.eduhttps://authors.library.caltech.edu/records/j15s9-ypk32", "eprint_id": 9554, "eprint_status": "archive", "datestamp": "2023-08-21 22:28:55", "lastmod": "2023-10-16 22:21:15", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Schroeder-W-A", "name": { "family": "Schroeder", "given": "W. A." } }, { "id": "Honnen-L", "name": { "family": "Honnen", "given": "Lewis" } }, { "id": "Green-F-C", "name": { "family": "Green", "given": "F. Charlotte" } } ] }, "title": "Chromatographic separation and identification of some peptides in partial hydroylsates of gelatin", "ispublished": "pub", "full_text_status": "public", "note": "\u00a9 1953 by the National Academy of Sciences. \n\nCommunicated by Linus Pauling, November 4, 1952. \n\nThis investigation was supported in part by a grant-in-aid from E. I. du Pont de Nemours and Company. Gates and Crellin Laboratories of Chemistry, Contribution No. 1748.", "abstract": "Recently we have been engaged in a study of the chemical structure of collagen and gelatin with the object of determining the sequence of the amino acid residues in the polypeptide chains of these proteins. In the course of this study we have made considerable progress in the chromatographic analysis of complex mixtures of peptides and we have isolated and identified several simple peptides which occur in partial hydrolysates of gelatin. The initial separation of the mixture into zones of one or more peptides has been made on a column of ion exchange resin; further separation of the peptides in each zone has been achieved by chromatographing in the form of dinitrophenyl (DNP) peptides on columns of silicic acid-Celite. It is to be hoped that the particular combination of chromatographic methods which has been successfully used in the present study will be helpful in the resolution of the complex mixtures which result from the partial hydrolysis of other proteins.", "date": "1953-01-01", "date_type": "published", "publication": "Proceedings of the National Academy of Sciences of the United States of America", "volume": "39", "number": "1", "publisher": "National Academy of Sciences", "pagerange": "23-30", "id_number": "CaltechAUTHORS:SCHRpnas53", "issn": "0027-8424", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:SCHRpnas53", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "primary_object": { "basename": "SCHRpnas53.pdf", "url": "https://authors.library.caltech.edu/records/j15s9-ypk32/files/SCHRpnas53.pdf" }, "resource_type": "article", "pub_year": "1953", "author_list": "Schroeder, W. A.; Honnen, Lewis; et el." }, { "id": "https://authors.library.caltech.eduhttps://authors.library.caltech.edu/records/dhp60-dkb46", "eprint_id": 91109, "eprint_status": "archive", "datestamp": "2023-08-19 01:58:28", "lastmod": "2023-10-19 22:09:57", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Schroeder-W-A", "name": { "family": "Schroeder", "given": "W. A." } } ] }, "title": "Sequence of four amino acids at the end of the single polypeptide chain of lysozyme", "ispublished": "pub", "full_text_status": "restricted", "note": "\u00a9 1952 American Chemical Society. \n\nReceived November 15, 1951.", "abstract": "During the investigation of DNP-lysozyme in which the end group of lysozyme was found to be lysine, a DNP-peptide (or peptides) was also isolated from certain hydrolysates. The fact that this DNP-peptide material yielded \u03b1,\u03b5-di-DNP-lysine on complete hydrolysis lead to the conclusion that it is derived from the amino end of the lysosyme molecule. Further study has now been made of this peptide material and hydrolytic conditions have been found which cause DNP-lysozyme to yield some DNP-tetrapeptide as well as shorter DNP-peptides. Analysis of the tetrapeptide and of the smaller peptides has shown that the tetrapeptide has the composiition of \u03b1,\u03b5-di-DNP-lysyl-valyl-phenylalanyl-glycine.", "date": "1952-01-05", "date_type": "published", "publication": "Journal of the American Chemical Society", "volume": "74", "number": "1", "publisher": "American Chemical Society", "pagerange": "281-282", "id_number": "CaltechAUTHORS:20181120-153101033", "issn": "0002-7863", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:20181120-153101033", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "collection": "CaltechAUTHORS", "other_numbering_system": { "items": [ { "id": "1622", "name": "Gates and Crellin Laboratories of Chemistry" } ] }, "doi": "10.1021/ja01121a528", "resource_type": "article", "pub_year": "1952", "author_list": "Schroeder, W. A." }, { "id": "https://authors.library.caltech.eduhttps://authors.library.caltech.edu/records/gs62h-a9659", "eprint_id": 10046, "eprint_status": "archive", "datestamp": "2023-08-21 22:20:29", "lastmod": "2023-10-16 22:38:38", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Schroeder-W-A", "name": { "family": "Schroeder", "given": "W. A." } }, { "id": "Kay-L-M", "name": { "family": "Kay", "given": "Lois M." } }, { "id": "Wells-I-C", "name": { "family": "Wells", "given": "Ibert C." } }, { "id": "Gerke-C", "name": { "family": "Gerke", "given": "Carolyn" } }, { "id": "Moss-J", "name": { "family": "Moss", "given": "James" } } ] }, "title": "Amino acid composition of hemoglobins of normal Negroes and sickle-cell anemics", "ispublished": "pub", "full_text_status": "public", "note": "Copyright \u00a9 1950 by the American Society for Biochemistry and Molecular Biology. \n\nReceived for publication, April 10, 1950. \n\nThe authors wish to express their appreciation of the interest and helpfulness of Professor Linus Pauling and Professor Robert B. Corey throughout the course of this work. Dr. Stanford Moore and Dr. William H. Stein have aided the chromatographic work with many useful suggestions. \n\n[I.C.W. was a] Postdoctoral Fellow of the Division of Medical Sciences of the National Research Council. \n\nGates and Crellin Laboratories of Chemistry, Contribution No. 1408.", "abstract": "The recent electrophoretic experiments of Pauling, Itano, Singer, and Wells (1) have demonstrated that the hemoglobins of normal Negroes and of sickle-cell anemics are unlike; in a buffer of suitable pH the two components of a mixture of these hemoglobins migrate in opposite directions. On the basis of the difference in their isoelectric points, it was concluded that the hemoglobin of sickle-cell anemics has 2 to 4 more net positive charges per molecule than normal hemoglobin. There is evidence that the composition of the heme moiety is the same in both proteins; one hypothesis which has been advanced to explain the dissimilarity of the two hemoglobins assumes a difference in the number or kind of ionizable groups in the molecules, that is, in the acidic or basic amino acids of the globin. Thus, the observed difference in charge might result from a small decrease in the number of acidic amino acids or a small increase in the number of basic amino acids in the molecule of sickle-cell hemoglobin relative to that of normal hemoglobin or from relatively large alterations in amino acid content in which the charges were almost compensated. \n\nThe object of the present study was to determine the amino acid composition of the two hemoglobins in order to ascertain the validity of this hypothesis. The analysis was made by means of the methods of starch chromatography which have recently been developed by Moore and Stein (2-6). The hydrolysates of two independently prepared samples of normal carbonmonoxyhemoglobin (to be referred to as N-Hb) and one sample of sickle-cell anemia hemoglobin (SC-Hb) have been analyzed. Approximately ten to fifteen individual determinations of each of seventeen amino acids and ammonia have been made by means of about 70 starch chromatograms.", "date": "1950-11-01", "date_type": "published", "publication": "Journal of Biological Chemistry", "volume": "187", "number": "1", "publisher": "American Society for Biochemistry and Molecular Biology", "pagerange": "221-240", "id_number": "CaltechAUTHORS:SCHRjbc50", "issn": "0021-9258", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:SCHRjbc50", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "primary_object": { "basename": "SCHRjbc50.pdf", "url": "https://authors.library.caltech.edu/records/gs62h-a9659/files/SCHRjbc50.pdf" }, "resource_type": "article", "pub_year": "1950", "author_list": "Schroeder, W. A.; Kay, Lois M.; et el." }, { "id": "https://authors.library.caltech.eduhttps://authors.library.caltech.edu/records/hzrmd-az076", "eprint_id": 88322, "eprint_status": "archive", "datestamp": "2023-08-19 01:00:51", "lastmod": "2023-10-18 21:58:10", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Zechmeister-L", "name": { "family": "Zechmeister", "given": "L." } }, { "id": "LeRosen-A-L", "name": { "family": "LeRosen", "given": "A. L." } }, { "id": "Schroeder-W-A", "name": { "family": "Schroeder", "given": "W. A." } }, { "id": "Polg\u00e1r-A", "name": { "family": "Polg\u00e1r", "given": "A." } }, { "id": "Pauling-L", "name": { "family": "Pauling", "given": "Linus" } } ] }, "title": "Spectral Characteristics and Configuration of Some Stereoisomeric Carotenoids Including Prolycopene and Pro-\u03b3-carotene", "ispublished": "pub", "full_text_status": "restricted", "note": "\u00a9 1943 American Chemical Society. \n\nReceived June 1, 1943. \n\nThe authors are indebted to Professor A. J. Haagen-Smit and Dr. G. Oppenheimer for analyses including catalytic microhydrogenations.", "abstract": "[no abstract]", "date": "1943-10", "date_type": "published", "publication": "Journal of the American Chemical Society", "volume": "65", "number": "10", "publisher": "American Chemical Society", "pagerange": "1940-1951", "id_number": "CaltechAUTHORS:20180727-101437995", "issn": "0002-7863", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:20180727-101437995", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "other_numbering_system": { "items": [ { "id": "932", "name": "Gates and Crellin Laboratories of Chemistry" } ] }, "doi": "10.1021/ja01250a039", "resource_type": "article", "pub_year": "1943", "author_list": "Zechmeister, L.; LeRosen, A. L.; et el." }, { "id": "https://authors.library.caltech.eduhttps://authors.library.caltech.edu/records/dva4r-yhs40", "eprint_id": 10833, "eprint_status": "archive", "datestamp": "2023-08-21 21:59:56", "lastmod": "2023-10-16 23:07:44", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Zechmeister-L", "name": { "family": "Zechmeister", "given": "L." } }, { "id": "Schroeder-W-A", "name": { "family": "Schroeder", "given": "W. A." } } ] }, "title": "The fruit of Pyracantha angustifolia: a practical source of pro-\u03b3-carotene and prolycopene", "ispublished": "pub", "full_text_status": "public", "note": "Copyright \u00a9 1942 by the American Society for Biochemistry and Molecular Biology. \n\n(Received for publication, April 13, 1942) \n\nGates and Crellin Laboratories of Chemistry, Contribution No. 880. \n\nWe wish to thank Dr. W. Hertrich, Curator of the Huntington Botanical Garden, for his courtesy, and Dr. G. Oppenheimer as well as Mr. G. Swinehart for the microanalyses.", "abstract": "Ripe fruit of Pyracantha (Cotoneaster) angustifolia Schneid. constitutes the best practical source for the isolation of pro-\u03b3-carotene, C40H56, and a good source for prolycopene, C40H56, both of which possess partially cis configurations. The yields were 27.7 mg. of crystallized pro-\u03b3-carotene and 28.4 mg. of prolycopene from 1 kilo of air-dried berries. A close stereoisomer of prolycopene was also isolated (7.3 mg.) and a monohydroxy pro-\u03b3-carotene observed in solution.", "date": "1942-07-01", "date_type": "published", "publication": "Journal of Biological Chemistry", "volume": "144", "number": "2", "publisher": "American Society for Biochemistry and Molecular Biology", "pagerange": "315-320", "id_number": "CaltechAUTHORS:ZECjbc42a", "issn": "0021-9258", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:ZECjbc42a", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "primary_object": { "basename": "ZECjbc42a.pdf", "url": "https://authors.library.caltech.edu/records/dva4r-yhs40/files/ZECjbc42a.pdf" }, "resource_type": "article", "pub_year": "1942", "author_list": "Zechmeister, L. and Schroeder, W. A." } ]