[ { "id": "https://authors.library.caltech.edu/records/1pf9e-cke65", "eprint_id": 10806, "eprint_status": "archive", "datestamp": "2023-08-21 23:41:39", "lastmod": "2023-10-16 23:06:52", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Rittenberg-M-B", "name": { "family": "Rittenberg", "given": "Marvin B." } }, { "id": "Campbell-D-H", "name": { "family": "Campbell", "given": "Dan H." } } ] }, "title": "Heterologous carriers in the anamnestic antihapten response", "ispublished": "pub", "full_text_status": "public", "note": "\u00a9 1968 by The Rockefeller University Press. RUP grants the public the non-exclusive right to copy, distribute, or display the Work under a Creative Commons Attribution\u2013Noncommercial\u2013Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/ and http://creativecommons.org/licenses/by-nc-sa/3.0/legalcode. \n\nSubmitted on December 10, 1967. \n\nThe authors gratefully acknowledge the excellent assistance of Mr. Bror Clark, Mr. Urs Rutishanser, Miss Jan Williams, and Miss Katherine Pratt. We wish to thank Dr. A. Malley and Dr. A.A. Amkraut for critically reading this manuscript, and Dr. G. Strejan for helpful discussions during the course of the investigation. \n\nThis investigation was supported in part by Grant AI 1355-19 from the National Institute of Allergy and Infectious Diseases and by a Hartford Foundation Grant. \n\n[M.R.B. was a] Leukemia Society Scholar. A portion of this work was carried out by Dr. Rittenberg during tenure of a National Institutes of Health Postdoctoral Fellowship at the California Institute of Technology. \n\nGates and Crellin Laboratories of Chemistry, Contribution 3614.\n\n
Published - RITjem68.pdf
", "abstract": "Anamnestic antihapten responses were obtained to trinitrophenyl (TNP) when rabbits sensitized to trinitrophenyl-hemocyanin (TNP-KLH) were challenged with TNP-heterologous protein conjugates. Hapten-heterologous carrier conjugates elicited antihapten titers similar in magnitude to those elicited by the homologous carrier conjugate. Hapten-heterologous carrier recall of antihapten was successful as early as 37 days and as late as 11 months after sensitization. There was no correlation between anti-TNP-precipitating antibody titer after sensitization and the ability to respond to challenge by hapten-heterologous carrier. The results are discussed in terms of immunogenicity of sensitization, suppressive effects of persisting postsensitization antibody, and submolecular haptenic environment as factors possibly affecting the heterologous recall process.", "date": "1968-04", "date_type": "published", "publication": "Journal of Experimental Medicine", "volume": "127", "number": "4", "publisher": "Rockefeller University Press", "pagerange": "717-730", "id_number": "CaltechAUTHORS:RITjem68", "issn": "0022-1007", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:RITjem68", "rights": "RUP grants the public the non-exclusive right to copy, distribute, or display the Work under a Creative Commons Attribution\u2013Noncommercial\u2013Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/ and http://creativecommons.org/licenses/by-nc-sa/3.0/legalcode.", "funders": { "items": [ { "agency": "NIH", "grant_number": "AI 1355-19" }, { "agency": "Hartford Foundation" }, { "agency": "Leukemia Society of America" }, { "agency": "NIH Postdoctoral Fellowship" } ] }, "other_numbering_system": { "items": [ { "id": "364", "name": "Caltech Gates and Crellin Laboratories of Chemistry" } ] }, "doi": "10.1084/jem.127.4.717", "pmcid": "PMC2138479", "primary_object": { "basename": "RITjem68.pdf", "url": "https://authors.library.caltech.edu/records/1pf9e-cke65/files/RITjem68.pdf" }, "resource_type": "article", "pub_year": "1968", "author_list": "Rittenberg, Marvin B. and Campbell, Dan H." }, { "id": "https://authors.library.caltech.edu/records/bf4yj-q2q04", "eprint_id": 34269, "eprint_status": "archive", "datestamp": "2023-08-19 05:37:00", "lastmod": "2023-10-19 14:48:30", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Garvey-J-S", "name": { "family": "Garvey", "given": "Justine S." } }, { "id": "Campbell-D-H", "name": { "family": "Campbell", "given": "Dan H." } }, { "id": "Das-M-L", "name": { "family": "Das", "given": "Manik L." } } ] }, "title": "Urinary excretion of foreign antigens and RNA following primary and secondary injections of antigens", "ispublished": "pub", "full_text_status": "public", "note": "\u00a9 1967 The Rockefeller University Press. \n\nSubmitted: 17 August 1966.\n\nThis investigation was supported by the National Institute of Allergy and Infectious Diseases.\n\nThe assistance of Mr. Bror Clark, Mr. David Acker, Mrs. Yvonne Matesich, and Mrs. Berta Weliky is gratefully acknowledged.\n\nPublished - GARjem67.pdf
", "abstract": "The following investigation was divided into two parts. The first was concerned with the rate and amount of excretion of soluble ^(35)S-labeled hemocyanin (KLH) and bovine serum albumin (BSA) following a single intravenous injection\ninto normal rabbits and also with the properties of the excreted antigen material and its possible association with ribonucleic acid (RNA) or nucleotides. The second involved the release and excretion of ^(35)S-labeled material which remained in tissues, or extravascular spaces, at 7 days following the primary injection. This release was accomplished by injection of the unlabeled native protein antigen as described previously by Garvey and Campbell (1).\nIn a recent report by Garvey and Campbell (2) the loss of antigen material from hepatic tissue following a secondary injection of the native protein carrier was clearly demonstrated by radioautography. Although much of the released material was taken up by spleen and lymph nodes, some of it escaped through the kidneys. It should be pointed out that the radioautographic studies did not bear out the speculation presented by Campbell and Garvey (3, 4) that release of primary antigen resulted in uptake by adjacent hepatic cells and thus production of a \"clone.\" However it is possible that clones of cells might be\nformed in lymphoid tissues by such a mechanism of release and transfer of antigen. The level may be too low for detection but still significant with respect to antibody formation. It was expected that the present study of excreted material would give further information as to the nature of retained antigen and also provide material\nfor future investigation of the biological properties of the released material.", "date": "1967-01-01", "date_type": "published", "publication": "Journal of Experimental Medicine", "volume": "125", "number": "1", "publisher": "Rockefeller University Press", "pagerange": "111-126", "id_number": "CaltechAUTHORS:20120920-132932683", "issn": "0022-1007", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:20120920-132932683", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "National Institute of Allergy and Infectious Diseases" }, { "agency": "NIH" } ] }, "other_numbering_system": { "items": [ { "id": "3398", "name": "Gates & Crellin Laboratories of Chemistry Contribution" } ] }, "doi": "10.1084/jem.125.1.111", "pmcid": "PMC2138346", "primary_object": { "basename": "GARjem67.pdf", "url": "https://authors.library.caltech.edu/records/bf4yj-q2q04/files/GARjem67.pdf" }, "resource_type": "article", "pub_year": "1967", "author_list": "Garvey, Justine S.; Campbell, Dan H.; et el." }, { "id": "https://authors.library.caltech.edu/records/y5z1f-w6f03", "eprint_id": 7055, "eprint_status": "archive", "datestamp": "2023-08-21 23:31:34", "lastmod": "2023-10-16 20:41:14", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Amkraut-A-A", "name": { "family": "Amkraut", "given": "Alfred A." } }, { "id": "Garvey-J-S", "name": { "family": "Garvey", "given": "Justine S." } }, { "id": "Campbell-D-H", "name": { "family": "Campbell", "given": "Dan H." } } ] }, "title": "Competition of haptens", "ispublished": "pub", "full_text_status": "public", "note": "\u00a9 1966 by The Rockefeller University Press \n\n(Received for publication 14 April 1966) \n\nThe authors wish to acknowledge the technical assistance of Mr. Bror Clark. We also wish to thank Dr. Arthur Malley for ultracentrifugal analyses and Dr. Marvin Rittenberg and Dr. George Hammond for critical comments. \n\nSupported by the United States Air Force through a National Academy of Science-National Research Council fellowship (Alfred A. Amkraut), and by Grant AI-1355 from the National Institute of Allergy and Infectious Diseases. Preliminary data were presented to the American Association of Immunologists, Atlantic City, April, 1964. \n\nFrom the Gates and Crellin Laboratories of Chemistry, Contribution No. 3367.\n\nPublished - AMKjem66.pdf
", "abstract": "Groups of rabbits were injected with either bovine serum albumin, sheep red cell stroma, or keyhole limpet hemocyanin to which 2,4-dinitrophenyl and/or p-azophenyl arsonate groups had been coupled. Groups of animals received either doubly coupled antigen or an equivalent mixture of singly coupled antigens. Materials were injected intravenously as a solution or subcutaneously and intramuscularly in complete Freund's adjuvant.\n\nThe presence of dinitrophenyl groups on the immunizing antigen could suppress, partially or completely, the antibody response to p-azophenyl arsonate when this hapten was located on the same molecule. Suppression was dependent on the ratio of haptenic groups on the molecule, appeared to be greatly affected by the method of immunization, and could be demonstrated in all three antigen systems. Partial suppression was manifested in decreased frequency and delayed appearance of the response as well as decreased maximal antibody titers. These findings appear irreconcilable with the possibility of direct clonal selection of antibody-producing cells by unprocessed antigen.", "date": "1966-09", "date_type": "published", "publication": "Journal of Experimental Medicine", "volume": "124", "number": "3", "publisher": "Rockefeller University Press", "pagerange": "293-306", "id_number": "CaltechAUTHORS:AMKjem66", "issn": "0022-1007", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:AMKjem66", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "National Academy of Sciences" }, { "agency": "National Research Council" }, { "agency": "NIH", "grant_number": "AI-1355" } ] }, "other_numbering_system": { "items": [ { "id": "3367", "name": "Caltech Gates and Crellin Laboratories of Chemistry" } ] }, "doi": "10.1084/jem.124.3.293", "pmcid": "PMC2138237", "primary_object": { "basename": "AMKjem66.pdf", "url": "https://authors.library.caltech.edu/records/y5z1f-w6f03/files/AMKjem66.pdf" }, "resource_type": "article", "pub_year": "1966", "author_list": "Amkraut, Alfred A.; Garvey, Justine S.; et el." }, { "id": "https://authors.library.caltech.edu/records/p30kj-t4344", "eprint_id": 4414, "eprint_status": "archive", "datestamp": "2023-08-21 22:52:41", "lastmod": "2023-10-16 17:44:46", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Garvey-J-S", "name": { "family": "Garvey", "given": "Justine S." } }, { "id": "Campbell-D-H", "name": { "family": "Campbell", "given": "Dan H." } } ] }, "title": "The in vivo stability of antibody", "ispublished": "pub", "full_text_status": "public", "note": "\u00a9 1959, by The Rockefeller Institute. \n\n(Received for publication, April 24, 1959) \n\nThe authors wish to express their appreciation for the very capable assistance of Mr. Bror Clark, Miss Rebecca Kent, and Mrs. Carla McNeill and the suggestions given by various members of the immunochemistry group. \n\nThis work was supported by the National Institutes of Health and The Rockefeller Foundation. \n\nContribution 2455 from the Division of Chemistry and Chemical Engineering, The California Institute of Technology, Pasadena\n\nPublished - 355.pdf
", "abstract": "Our previous studies, concerned largely with antigen retention and the characterization of antigen in tissues, led us to suspect that some antibody, like antigen, may be stabilized in tissue sites (1). The purpose of the present investigation was to study further, such antibody which appeared to be bound with antigen and perhaps normal tissue constituents. The investigation was carried out in the following manner: rabbits were first immunized by a series of intravenous injections of antigen and at the height of precipitin production they were fed S35-labelled yeast cells. Newly produced antibody, like the other plasma proteins, became readily labelled with S35 amino acids within a few hours. After varying lengths of time, when circulating antibody had declined, antigen was again injected. Serum samples were then taken at various intervals and the specific activity of antibody was measured as soon as antibody reappeared in the circulation. The specific activity of antibody was measured in the antigen-antibody precipitates obtained, both in the period when the antibody had been allowed to decline and also after antigen had been reinjected to induce an anamnestic response. A comparison of antibody-specific activity provided evidence that there was a release of antibody which had been made at the time of S35 feeding and stored in some stabilized form in tissues. The results are discussed with respect to the anamnestic response and the retention of antigen in tissues.", "date": "1959-09", "date_type": "published", "publication": "Journal of Experimental Medicine", "volume": "110", "number": "3", "publisher": "Rockefeller University Press", "pagerange": "355-368", "id_number": "CaltechAUTHORS:GARjem59", "issn": "0022-1007", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:GARjem59", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "NIH" }, { "agency": "Rockefeller Foundation" } ] }, "other_numbering_system": { "items": [ { "id": "2455", "name": "Caltech Division of Chemistry and Chemical Engineering" } ] }, "doi": "10.1084/jem.110.3.355", "pmcid": "PMC2137007", "primary_object": { "basename": "355.pdf", "url": "https://authors.library.caltech.edu/records/p30kj-t4344/files/355.pdf" }, "resource_type": "article", "pub_year": "1959", "author_list": "Garvey, Justine S. and Campbell, Dan H." }, { "id": "https://authors.library.caltech.edu/records/4wzvs-20997", "eprint_id": 4411, "eprint_status": "archive", "datestamp": "2023-08-21 22:50:01", "lastmod": "2023-10-16 17:44:39", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Ishizaka-K", "name": { "family": "Ishizaka", "given": "Kimishige" } }, { "id": "Ishizaka-T", "name": { "family": "Ishizaka", "given": "Teruko" } }, { "id": "Campbell-D-H", "name": { "family": "Campbell", "given": "Dan H." } } ] }, "title": "The biological activity of soluble antigen-antibody complexes: II. Physical properties of soluble complexes having skin-irritating activity", "ispublished": "pub", "full_text_status": "public", "note": "\u00a9 1959, by The Rockefeller Institute. \n\n(Received for publication, September 24, 1958) \n\nThis work was supported in part by a grant from the National Institute of Allergy and Infectious Diseases and in part by The Rockefeller Foundation. The authors wish to acknowledge the helpful advice and criticisms of Doctors D. W. Talmage, S. J. Singer, I. L. Trapani, and W. E. Vannier, and the technical assistance of Mr. Bror Clark. \n\nContribution No. 2402 from the Division of Chemistry and Chemical Engineering, The California Institute of Technology, Pasadena\n\nPublished - ISHjem59.pdf
", "abstract": "Previous work by Germuth and McKinnon (1), Trapani et al. (2), and ourselves (3) has established the fact that soluble antigen-antibody complexes formed in excess antigen can, (a) induce symptoms similar to anaphylaxis, (b) cause contraction of isolated smooth muscle from normal guinea pigs, and (c) increase the permeability of skin capillaries in a manner similar to that obtained in passive cutaneous anaphylaxis. These findings immediately raise many questions as to the fundamental mechanisms involved. For example, is the free antigen playing some role; is the toxicity dependent upon some change in the molecular structure of either antigen or antibody upon combination; is the complex itself toxic without any change in the molecular structure of the components; is the antigen-antibody ratio important; and, is complement involved? The work reported here involves a study of the possible role of free antigen and the nature of the complex. Some study was also made of untreated and decomplemented antiserums and, although there was no difference, this cannot rule out the possible participation of the test animal's (guinea pig's) own complement.", "date": "1959-02", "date_type": "published", "publication": "Journal of Experimental Medicine", "volume": "109", "number": "2", "publisher": "Rockefeller University Press", "pagerange": "127-143", "id_number": "CaltechAUTHORS:ISHjem59", "issn": "0022-1007", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:ISHjem59", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "NIH" }, { "agency": "Rockefeller Foundation" } ] }, "other_numbering_system": { "items": [ { "id": "2402", "name": "Caltech Division of Chemistry and Chemical Engineering" } ] }, "doi": "10.1084/jem.109.2.127", "pmcid": "PMC2136941", "primary_object": { "basename": "ISHjem59.pdf", "url": "https://authors.library.caltech.edu/records/4wzvs-20997/files/ISHjem59.pdf" }, "resource_type": "article", "pub_year": "1959", "author_list": "Ishizaka, Kimishige; Ishizaka, Teruko; et el." }, { "id": "https://authors.library.caltech.edu/records/pny1d-a8131", "eprint_id": 50387, "eprint_status": "archive", "datestamp": "2023-09-15 04:51:56", "lastmod": "2023-10-23 21:10:44", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Garvey-J-S", "name": { "family": "Garvey", "given": "Justine S." } }, { "id": "Campbell-D-H", "name": { "family": "Campbell", "given": "Dan H." } } ] }, "title": "Effect of secondary injections of antigen upon the retention in liver of a primary injection", "ispublished": "pub", "full_text_status": "public", "note": "\u00a9 1958 Rockefeller University Press. Received for publication, October 3, 1957. Submitted: 2 October 1957.\n\nThis work was supported by the National Institutes of Health and The Rockefeller Foundation.\n\nThe authors wish to express their appreciation of the technical assistance of Mr. Bror Clark.\n\nPublished - GARjem58.pdf
", "abstract": "The retention of antigen in rabbit liver tissue, resulting from a primary intravenous injection, is influenced by immunization brought about by subsequent intravenous injections of the same antigen. In rabbits given a single primary intravenous injection of radioactive antigen, the retention of radioactivity in liver tissue, after a period of 21 days, was greater than when the primary injection was followed by secondary injections of the same, but non-radioactive antigen. The results were similar for both S^(35)-azohemocyanin and S^(35)-azo-bovine-serum-albumin, except the hemocyanin was retained to a greater extent than the albumin.\n\nThere was very little if any correlation between the number of secondary injections and retention of the initial injection. Quantitative antibody nitrogen data, obtained for the serum of each rabbit showed, in general, an inverse relationship between circulating antibody and radioactivity retained, i.e. the higher the circulating antibody titer, the lower the retention of radioactivity in liver tissue.\n\nPassively administered homologous antibody did not produce a change in the retention of the primary injection of antigen nor did secondary injections of a heterologous native protein injected according to the same immunization schedule as the homologous azoprotein. From these results it may be concluded that an intracellular antibody-forming activity influences the loss (or retention) of antigen deposited in liver tissue and that the mechanism is immunologically specific.", "date": "1958-04", "date_type": "published", "publication": "Journal of Experimental Medicine", "volume": "107", "number": "4", "publisher": "Rockefeller University Press", "pagerange": "497-506", "id_number": "CaltechAUTHORS:20141015-065108808", "issn": "0022-1007", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:20141015-065108808", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "NIH" }, { "agency": "Rockefeller Foundation" } ] }, "other_numbering_system": { "items": [ { "id": "2252", "name": "Caltech Division of Chemistry and Chemical Engineering" } ] }, "doi": "10.1084/jem.107.4.497", "pmcid": "PMC2136838", "primary_object": { "basename": "GARjem58.pdf", "url": "https://authors.library.caltech.edu/records/pny1d-a8131/files/GARjem58.pdf" }, "resource_type": "article", "pub_year": "1958", "author_list": "Garvey, Justine S. and Campbell, Dan H." }, { "id": "https://authors.library.caltech.edu/records/en35h-0y812", "eprint_id": 50384, "eprint_status": "archive", "datestamp": "2023-09-15 04:51:51", "lastmod": "2023-10-23 21:10:42", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Garvey-J-S", "name": { "family": "Garvey", "given": "Justine S." } }, { "id": "Campbell-D-H", "name": { "family": "Campbell", "given": "Dan H." } } ] }, "title": "The Retention of S^(35)-Labelled Bovine Serum Albumin in\n Normal and Immunized rabbit Liver Tissue", "ispublished": "pub", "full_text_status": "public", "note": "\u00a9 1957 Rockefeller University Press. Received for publication, January 7, 1957. Submitted: 6 January 1957.\n\nThis work was supported by the National Institutes of Health and The Rockefeller Foundation.\n\nThe authors wish to express their appreciation of the technical assistance of Mr. Bror Clark and Mr. Daniel L. Wulff.\n\nPublished - GARjem57.pdf
", "abstract": "The S^(35)-label of S^(35)-BSA was detected in the liver tissue of rabbits to the extent of 0.02 per cent (10 \u00b5g or \u2243 10^(14) molecules) of the injected material at 140 days after injection.\nThe rate of loss of antigen at the termination of the experiment was of such an order that significant amounts would be expected to persist for at least several years.\nData are reported which extend the retention data previously reported on S^(35)-labelled hemocyanin. They indicate that amounts of the order of 0.05 per cent (25 \u00b5g.) of antigen material persist at 330 days after injection.\nAll of the radioactivity of material retained in the liver tissue 6 weeks after injection was immunologically related to the original S^(35)-BSA antigen.\nPreliminary studies are reported which indicate that the retained antigen is bound to ribonucleic acid.\nA new method is described for the isolation of p-azophenylsulfonate bovine serum albumin from tissue extracts by means of a Dowex 2 adsorbent.", "date": "1957-04", "date_type": "published", "publication": "Journal of Experimental Medicine", "volume": "105", "number": "4", "publisher": "Rockefeller University Press", "pagerange": "361-372", "id_number": "CaltechAUTHORS:20141014-151631021", "issn": "0022-1007", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:20141014-151631021", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "NIH" }, { "agency": "Rockefeller Foundation" } ] }, "other_numbering_system": { "items": [ { "id": "2154", "name": "Caltech Gates and Crellin Laboratories of Chemistry" } ] }, "doi": "10.1084/jem.105.4.361", "pmcid": "PMC2136700", "primary_object": { "basename": "GARjem57.pdf", "url": "https://authors.library.caltech.edu/records/en35h-0y812/files/GARjem57.pdf" }, "resource_type": "article", "pub_year": "1957", "author_list": "Garvey, Justine S. and Campbell, Dan H." }, { "id": "https://authors.library.caltech.edu/records/dj2yy-rtj92", "eprint_id": 6644, "eprint_status": "archive", "datestamp": "2023-08-21 22:42:17", "lastmod": "2023-10-16 20:27:05", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Garvey-J-S", "name": { "family": "Garvey", "given": "Justine S." } }, { "id": "Campbell-D-H", "name": { "family": "Campbell", "given": "Dan H." } } ] }, "title": "The retention of S35-labelled bovine serum albumin on normal and immunized rabbit liver tissue", "ispublished": "pub", "full_text_status": "public", "note": "\u00a9 1957, by The Rockefeller Institute for Medical Research New York. \n\n(Received for publication, January 7, 1957) \n\nThe authors wish to express their appreciation of the technical assistance of Mr. Bror Clark and Mr. Daniel L. Wulff. \n\nThe Gates and Crellin Laboratories of Chemistry, The California Institute of Technology, Pasadena) Contribution No. 2154. \n\nThis work was supported by the National Institutes of Health and The Rockefeller Foundation.\n\nPublished - GARjem57.pdf
", "abstract": "The S35-label of S35-BSA was detected in the liver tissue of rabbits to the extent of 0.02 per cent (10 \u00b5g or sime 1014 molecules) of the injected material at 140 days after injection. \n\nThe rate of loss of antigen at the termination of the experiment was of such an order that significant amounts would be expected to persist for at least several years. \n\nData are reported which extend the retention data previously reported on S35-labelled hemocyanin. They indicate that amounts of the order of 0.05 per cent (25 \u00b5g.) of antigen material persist at 330 days after injection. \n\nAll of the radioactivity of material retained in the liver tissue 6 weeks after injection was immunologically related to the original S35-BSA antigen. \n\nPreliminary studies are reported which indicate that the retained antigen is bound to ribonucleic acid. \n\nA new method is described for the isolation of p-azophenylsulfonate bovine serum albumin from tissue extracts by means of a Dowex 2 adsorbent.", "date": "1957-04", "date_type": "published", "publication": "Journal of Experimental Medicine", "volume": "105", "number": "4", "publisher": "Rockefeller University Press", "pagerange": "361-372", "id_number": "CaltechAUTHORS:GARjem57", "issn": "0022-1007", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:GARjem57", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "other_numbering_system": { "items": [ { "id": "2154", "name": "Caltech Gates and Crellin Laboratories of Chemistry" } ] }, "doi": "10.1084/jem.105.4.361", "pmcid": "PMC2136700", "primary_object": { "basename": "GARjem57.pdf", "url": "https://authors.library.caltech.edu/records/dj2yy-rtj92/files/GARjem57.pdf" }, "resource_type": "article", "pub_year": "1957", "author_list": "Garvey, Justine S. and Campbell, Dan H." }, { "id": "https://authors.library.caltech.edu/records/gq1vy-hcp76", "eprint_id": 11972, "eprint_status": "archive", "datestamp": "2023-08-21 22:23:42", "lastmod": "2023-10-17 16:01:19", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Campbell-D-H", "name": { "family": "Campbell", "given": "Dan H." } }, { "id": "Luescher-E", "name": { "family": "Luescher", "given": "Ernst" } }, { "id": "Lerman-L-S", "name": { "family": "Lerman", "given": "Leonard S." } } ] }, "title": "Immunologic adsorbents. I. Isolation of antibody by means of a cellulose-protein antigen", "ispublished": "pub", "full_text_status": "public", "note": "\u00a9 1951 by the National Academy of Sciences. \n\nCommunicated by Linus Pauling, July 16, 1951. \n\nThis work was supported in part by a grant from The Rockefeller Foundation and in part by a grant from the U.S. Public Health Service. \n\nGates and Crellin Laboratories of Chemistry, Contribution No. 1589.\n\nPublished - CAMpnas51.pdf
", "abstract": "For the past several years we have been interested in devising methods that would afford practical procedures for the isolation and purification of antibodies from immune serums and in particular the isolation of non-precipitating antibodies from animal serums and allergic antibodies (reagins) from human serums.(1) The general approach has been to attempt to produce an insoluble protein antigen which would combine specifically with antibody to give a complex that could be dissociated into soluble antibody and insoluble antigen, which could then be separated by centrifugation. Attempts were made to confer insolubility on protein antigens such as ovalbumin and crystalline bovine serum albumin without destroying their antigenicity. Products were obtained by use of the usual denaturing agents, tannic acid, and bifunctional coupling reagents (e.g., tetrazotized benzidine), and also by coupling to an insoluble substrate such as phenolic resins or insoluble proteins (such as fibrin). However, in every case the resulting product either had lost too much native antigenicity (i.e., adsorbed serum always contained antibody which reacted with native antigen), was too soluble, or had too much power of adsorption for non-specific protein.", "date": "1951-09", "date_type": "published", "publication": "Proceedings of the National Academy of Sciences of the United States of America", "volume": "37", "number": "9", "publisher": "National Academy of Sciences", "pagerange": "575-578", "id_number": "CaltechAUTHORS:CAMpnas51", "issn": "0027-8424", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:CAMpnas51", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "Rockefeller Foundation" }, { "agency": "Public Health Service" } ] }, "other_numbering_system": { "items": [ { "id": "1589", "name": "Gates and Crellin Laboratories of Chemistry" } ] }, "primary_object": { "basename": "CAMpnas51.pdf", "url": "https://authors.library.caltech.edu/records/gq1vy-hcp76/files/CAMpnas51.pdf" }, "resource_type": "article", "pub_year": "1951", "author_list": "Campbell, Dan H.; Luescher, Ernst; et el." }, { "id": "https://authors.library.caltech.edu/records/xsa81-frm61", "eprint_id": 5906, "eprint_status": "archive", "datestamp": "2023-08-21 22:19:59", "lastmod": "2023-10-16 19:58:13", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Lippman-R-W", "name": { "family": "Lippman", "given": "Richard W." } }, { "id": "Cameron-G", "name": { "family": "Cameron", "given": "Gladys" } }, { "id": "Campbell-D-H", "name": { "family": "Campbell", "given": "Dan H." } } ] }, "title": "The Specificity of Anti-Kidney Antibody Determined by Its Effect upon Tissue Culture Explants", "ispublished": "pub", "full_text_status": "public", "note": "Copyright \u00a9 1950 by the National Academy of Sciences \n\nCommunicated by Linus Pauling, August 1, 1950 \n\nThis work was aided by a research grant from the National Heart Institute, of the National Institutes of Health. Dr. Lippman is a Fellow of the John Simon Guggenheim Memorial Foundation. \n\nThe Gates and Crellin Laboratories of Chemistry, Contribution No. 1442.", "abstract": "While investigating the pathogenesis of experimental nephritis produced by rabbit anti-rat-kidney antibody, it occurred to us that the effects of antikidney antibody on kidney tissue might readily be visualized in tissue cultures. The specificity of tissue antigens has previously been investigated by the usual immunologic procedures [1] and the effects of antibodies [2,3] upon tissue explants has long been known. The growth and function of tissue explants have previously been used to study the specificity of tissue antibodies [4,5], but the antisera used were of low, uncertain potency, and only a few different tissues were examined in testing the toxic effects. The following study shows that rabbit anti-rat-kidney gamma globulin is toxic for tissue explants of brain and heart muscle, as well as kidney. These effects are of low species specificity and may be observed in cultures prepared from chick embryo tissues, as well as those prepared from rat tissues. In addition, the serum of patients with glomerular nephritis was found to contain a substance with similar effects and specificity.", "date": "1950-10-01", "date_type": "published", "publication": "Proceedings of the National Academy of Sciences of the United States of America", "volume": "36", "number": "10", "publisher": "National Academy of Sciences", "pagerange": "576-580", "id_number": "CaltechAUTHORS:LIPpnas50", "issn": "0027-8424", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:LIPpnas50", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "primary_object": { "basename": "LIPpnas50.pdf", "url": "https://authors.library.caltech.edu/records/xsa81-frm61/files/LIPpnas50.pdf" }, "resource_type": "article", "pub_year": "1950", "author_list": "Lippman, Richard W.; Cameron, Gladys; et el." }, { "id": "https://authors.library.caltech.edu/records/p7daq-8w294", "eprint_id": 12080, "eprint_status": "archive", "datestamp": "2023-08-21 22:03:46", "lastmod": "2023-10-17 16:30:57", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Johnson-F-H", "name": { "family": "Johnson", "given": "Frank H." } }, { "id": "Campbell-D-H", "name": { "family": "Campbell", "given": "Dan H." } } ] }, "title": "Pressure and protein denaturation", "ispublished": "pub", "full_text_status": "public", "note": "\u00a9 1946 American Society of Biological Chemists. \n \nReceived for publication, February 6, 1946. \n\nThe authors take pleasure in acknowledging the interest as well as lengthy discussions and assistance of Professor Linus Pauling in connection with this study. \n\n[F.H.J. was a] Fellow of the John Simon Guggenheim Memorial Foundation, from the Department of Biology, Princeton University, Princeton, New Jersey.\n\nPublished - JOHjbc46.pdf
", "abstract": "Kinetic analyses have indicated that moderate hydrostatic pressures, up to some 700 atmospheres, oppose reversible and irreversible denaturations of certain enzyme systems, apparent at temperatures above the normal optimum of the enzyme reaction, as well as at lower temperatures in the presence of denaturants such as alcohol (1-4). Qualitative observations have shown that such pressures also retard the precipitation of highly purified human serum globulin and egg albumin at 65\u00b0 (5) and slow the destruction of specific antitoxic activity at the same temperature (6). In this study we have obtained quantitative data with regard to the influence of various pressures, up to 10,000 pounds per sq. in., and of low concentrations of ethyl alcohol on the time course of precipitation of human serum globulin (1) at 65\u00b0 and pH 6.0.", "date": "1946-06", "date_type": "published", "publication": "Journal of Biological Chemistry", "volume": "163", "number": "3", "publisher": "American Society for Biochemistry and Molecular Biology", "pagerange": "689-698", "id_number": "CaltechAUTHORS:JOHjbc46", "issn": "0021-9258", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:JOHjbc46", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "John Simon Guggenheim Foundation" } ] }, "primary_object": { "basename": "JOHjbc46.pdf", "url": "https://authors.library.caltech.edu/records/p7daq-8w294/files/JOHjbc46.pdf" }, "resource_type": "article", "pub_year": "1946", "author_list": "Johnson, Frank H. and Campbell, Dan H." }, { "id": "https://authors.library.caltech.edu/records/spfr3-8j294", "eprint_id": 88330, "eprint_status": "archive", "datestamp": "2023-08-19 00:56:51", "lastmod": "2023-10-18 21:58:43", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Pauling-L", "name": { "family": "Pauling", "given": "Linus" } }, { "id": "Pressman-D", "name": { "family": "Pressman", "given": "David" } }, { "id": "Campbell-D-H", "name": { "family": "Campbell", "given": "Dan H." } }, { "id": "Ikeda-Carol", "name": { "family": "Ikeda", "given": "Carol" } }, { "id": "Ikawa-Miyoshi", "name": { "family": "Ikawa", "given": "Miyoshi" } } ] }, "title": "The Serological Properties of Simple Substances. I. Precipitation Reactions between Antibodies and Substances Containing Two or More Haptenic Groups", "ispublished": "pub", "full_text_status": "restricted", "note": "\u00a9 1942 American Chemical Society. \n\nReceived July 6, 1942. \n\nWe are grateful to the Rockefeller Foundation for financial support of this work. We wish to thank Mr. Paul Faust and Mr. Shelton Steinle for their assistance in carrying out analyses, and Mr. David Brown for the preparation of phenylarsonic acid.", "abstract": "The problem of obtaining from precipitation experiments evidence about the structure of antibodies and the nature of serological reactions is obviously greatly simplified by the replacement of protein antigens by simple substances of known structure. For this reason we began and are carrying on an extensive program of investigation of the reactions of simple substances with antisera. In this paper we report the quantitative study of the precipitin reaction for twenty simple substances containing two or more haptenic groups, and the results of tests of seven substances containing one group. It is found that the observations support the framework theory of serological precipitates.", "date": "1942-12", "date_type": "published", "publication": "Journal of the American Chemical Society", "volume": "64", "number": "12", "publisher": "American Chemical Society", "pagerange": "2994-3003", "id_number": "CaltechAUTHORS:20180727-101438826", "issn": "0002-7863", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:20180727-101438826", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "Rockefeller Foundation" } ] }, "other_numbering_system": { "items": [ { "id": "885", "name": "Gates and Crellin Laboratories of Chemistry" } ] }, "doi": "10.1021/ja01264a080", "resource_type": "article", "pub_year": "1942", "author_list": "Pauling, Linus; Pressman, David; et el." }, { "id": "https://authors.library.caltech.edu/records/htxq8-qe288", "eprint_id": 88331, "eprint_status": "archive", "datestamp": "2023-08-19 00:56:58", "lastmod": "2023-10-18 21:58:47", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Pauling-L", "name": { "family": "Pauling", "given": "Linus" } }, { "id": "Pressman-D", "name": { "family": "Pressman", "given": "David" } }, { "id": "Campbell-D-H", "name": { "family": "Campbell", "given": "Dan H." } }, { "id": "Ikeda-Carol", "name": { "family": "Ikeda", "given": "Carol" } } ] }, "title": "The Serological Properties of Simple Substances. II. The Effects of Changed Conditions and of Added Haptens on Precipitation Reactions of Polyhaptenic Simple Substances", "ispublished": "pub", "full_text_status": "restricted", "note": "\u00a9 1942 American Chemical Society. \n\nReceived July 6, 1942.", "abstract": "During the course of the investigation of precipitation reactions of polyhaptenic simple substances reported in the preceding paper of this series' we found it desirable to carry out a study of the effects of changed conditions of precipitation and washing on the amount of residual precipitate. We also made some experiments on the inhibition of precipitation by added haptens, in order to see how great would be the effects of monohaptenic impurities possibly present in the substances studied. The results obtained are presented and discussed in this paper.", "date": "1942-12", "date_type": "published", "publication": "Journal of the American Chemical Society", "volume": "64", "number": "12", "publisher": "American Chemical Society", "pagerange": "3003-3009", "id_number": "CaltechAUTHORS:20180727-101438922", "issn": "0002-7863", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:20180727-101438922", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "other_numbering_system": { "items": [ { "id": "886", "name": "Gates and Crellin Laboratories of Chemistry" } ] }, "doi": "10.1021/ja01264a081", "resource_type": "article", "pub_year": "1942", "author_list": "Pauling, Linus; Pressman, David; et el." }, { "id": "https://authors.library.caltech.edu/records/4eqmr-mpc59", "eprint_id": 4418, "eprint_status": "archive", "datestamp": "2023-08-21 22:00:06", "lastmod": "2023-10-16 17:44:55", "type": "article", "metadata_visibility": "show", "creators": { "items": [ { "id": "Pauling-L", "name": { "family": "Pauling", "given": "Linus" } }, { "id": "Campbell-D-H", "name": { "family": "Campbell", "given": "Dan H." } } ] }, "title": "The manufacture of antibodies in vitro", "ispublished": "pub", "full_text_status": "public", "note": "\u00a9 1942, by The Rockefeller Institute for Medical Research New York. \n\n(Received for publication, April 25, 1942) \n\nA brief statement of the results of these experiments has beea published: Pauling, L., and Campbell, D. H., Science, 1942, 95, 440. \n\nWe acknowledge with appreciation the financial support of this work by the Rockefeller Foundation. We are also indebted to Dr. David Pressman and Mr. Carol Ikeda of these Laboratories for help with the experiments, and to Dr. W. Goebel of The Rockefeller Institute for Medical Research, Dr. E. J. Cohn of Harvard Medical School, and Dr. J. D. Porsche of Armour and Co. for providing us with materials.\n\nPublished - PAUjem42.pdf
", "abstract": "A protein solution with the properties of a specific antiserum to the triphenylmethane dye methyl blue has been made by treating a solution of bovine gamma-globulin and the dye with alkali and then slowly neutralizing the alkali. Some success has been obtained also in the formation of antibodies from other serum proteins and by other denaturation-renaturation procedures. \n\nBy heating solutions of gamma-globulin and antigen to 57\u00b0C. for several days antisera homologous to the antigens have been prepared. This method has been used successfully with the azodye 1,3-dihydroxy-2,4,6-tri(p-azophenyl-arsonic acid) benzene and with pneumococcus polysaccharide Type III. The antipneumococcus sera were found to precipitate the polysaccharide of Type III but not those of Types I and VIII and to agglutinate pneumococci of Type III but not those of Types I and II.", "date": "1942-08", "date_type": "published", "publication": "Journal of Experimental Medicine", "volume": "76", "number": "2", "publisher": "Rockefeller University Press", "pagerange": "211-220", "id_number": "CaltechAUTHORS:PAUjem42", "issn": "0022-1007", "official_url": "https://resolver.caltech.edu/CaltechAUTHORS:PAUjem42", "rights": "No commercial reproduction, distribution, display or performance rights in this work are provided.", "funders": { "items": [ { "agency": "Rockefeller Foundation" } ] }, "doi": "10.1084/jem.76.2.211", "pmcid": "PMC2135224", "primary_object": { "basename": "PAUjem42.pdf", "url": "https://authors.library.caltech.edu/records/4eqmr-mpc59/files/PAUjem42.pdf" }, "resource_type": "article", "pub_year": "1942", "author_list": "Pauling, Linus and Campbell, Dan H." } ]