Skip to main content

The structure and biological activity of immunoglobulins and their subunits

  • Conference paper
  • First Online:
  • 35 Accesses

Part of the book series: Ergebnisse der Physiologie, biologischen Chemie und experimentellen Pharmakologie ((ERGEBPHYSIOL,volume 56))

This is a preview of subscription content, log in via an institution.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Andersen, B. R., andW. E. Vannier: The sedimentation properties of the skin-sensitizing antibodies of ragweed-sensitive patients. J. Exp. Med.120, 31 (1964).

    PubMed  CAS  Google Scholar 

  • Askonas, B. A., andJ. L. Fahey: An investigation of closely related γ-myeloma proteins and normal mouse γ-globulin by partial enzymatic degradation and starch-gel electrophoresis. Nature (Lond.)190, 980 (1961).

    CAS  Google Scholar 

  • Barandun, S., u.H. Isliker: Properdinbestimmungen im Serum von Patienten mit einem Antikörpermangelsyndrom (Hypo- und Agammaglobulinämie). In: 4th Colloquium, edit.H. Peeters, p. 205. Bruges: St. Jans Hospital 1956.

    Google Scholar 

  • —,P. Kistler, F. Jeunet, andH. Isliker: Intravenous administration of γ-globulin. Vox Sang. (Basel)7, 157 (1962).

    CAS  Google Scholar 

  • Benacerraf, B., Z. Ovary, K. J. Bloch, andE. C. Franklin: Properties of guinea pig 7S antibodies. I. Electrophoretic separation of two types of guinea pig 7S antibodies. J. Exp. Med.117, 937 (1963).

    PubMed  CAS  Google Scholar 

  • Binaghi, R. A., andB. Benacerraf: Properties of rat anaphylactic antibody. J. Immunol. (in press) (1964).

    Google Scholar 

  • ——,K. J. Bloch, andF. M. Kourilsky: Properties of rat anaphylactic antibody. J. Immunol.92, 927 (1964).

    PubMed  CAS  Google Scholar 

  • —,P. Liacopoulos, B. N. Halpern, andM. Liacopoulos-Briot: Interference of nonspecific γ-globulins with passive in vitro anaphylactic sensitization of isolated guineapig intestine. Immunology5, 204 (1962).

    PubMed  CAS  Google Scholar 

  • Blanc, B.: Les protéines du lactosérum. Leurs relations avec l’immunité et le métabolisme du fer. Thèse, Université de Lausanne 1962.

    Google Scholar 

  • Bloch, K. J., F. M. Kourilsky, Z. Ovary, andB. Benacerraf: Properties of guinea pig 7 S antibodies. III. Identification of antibodies involved in complement fixation and hemolysis. J. Exp. Med.117, 965 (1963).

    PubMed  CAS  Google Scholar 

  • Boyden, S. V.: Cytophilic antibody in guinea-pigs with delayed-type hypersensitivity. Immunology7, 474 (1964).

    PubMed  CAS  Google Scholar 

  • —, andE. Sorkin: The absorption of antibody and antigen by spleen cells in vitro. Some further experiments. Immunology4, 244 (1961).

    Google Scholar 

  • Brambell, F. W. R., W. A. Hemmings, C. L. Oakley, andR. R. Porter: The relative transmission of the fractions of papain-hydrolyzed homologous γ-globulin from the uterine cavity to the foetal circulation in the rabbit. Proc. roy. Soc.151, 478 (1959).

    Google Scholar 

  • Cann, J. R.: The separation and purification of antibodies. In: Immunity and virus infection, edit.F. Najjar, p. 100. New York: John Wiley & Sons 1959.

    Google Scholar 

  • Cebra, J. J., D. Givol, H. I. Silman, andE. Katchalski: A two-stage cleavage of rabbit γ-globulin by a water-insoluble papain preparation followed by cysteine. J. Biol. Chem.236, 1720 (1961).

    PubMed  CAS  Google Scholar 

  • Cerottini, J., J. C. Jaton, T. Froidevaux, etH. Isliker: Immunofluorescence à l’aide de fragments d’anticorps. Helv. physiol. pharmacol. Acta22, C9 (1964).

    PubMed  CAS  Google Scholar 

  • Cohen, S.: Properties of the separated chains of human γ-globulin. Nature (Lond.)197, 253 (1963).

    CAS  Google Scholar 

  • —, andT. Freeman: Metabolic heterogeneity of human gamma-globulins. Biochem. J.76, 475 (1960).

    PubMed  CAS  Google Scholar 

  • — andR. R. Porter: Heterogeneity of the peptide chains of γ-globulin. Biochem. J.90, 278 (1964).

    PubMed  CAS  Google Scholar 

  • Crumpton, H. J., andJ. M. Wilkinson: Amino acid compositions of human and rabbit γ-globulins and the fragments produced by reduction. Biochem. J.88, 228 (1963).

    PubMed  CAS  Google Scholar 

  • Deutsch, H. F., andJ. I. Morton: Dissociation of human serum macroglobulins. Science125, 600 (1957).

    PubMed  CAS  Google Scholar 

  • ——: Human serum macroglobulins and dissociation units. J. Biol. Chem.231, 1107 (1958).

    PubMed  CAS  Google Scholar 

  • —,E. R. Stiehm, andJ. I. Morton: Action of papain on human serum globulins. J. Biol. Chem.236, 2216 (1961).

    PubMed  CAS  Google Scholar 

  • Dixon, F.: The lack of absorption of ingested bovine antibody in humans. J. Immunol.83, 437 (1959).

    PubMed  CAS  Google Scholar 

  • Edelman, G. M.: Formation of active 7 S antibody molecules by reassociation of L and H polypeptide chains. Internat. Symposium on the cellular and molecular basis of antibody formation, Prague 1964.

    Google Scholar 

  • —, andB. Benacerraf: On structural and functional relations between antibodies and gamma-globulins. Proc. Nat. Acad. Sci. (Wash.)48, 1035 (1962).

    CAS  Google Scholar 

  • —, andJ. A. Gally: The nature of Bence-Jones proteins. Chemical similarities to polypeptide chains of myeloma globulins and normal γ-globulins. J. Exp. Med.116, 207 (1962).

    PubMed  CAS  Google Scholar 

  • ——: A model for the 7S antibody molecule. Proc. Nat. Acad. Sci. (Wash.)51, 846 (1964).

    CAS  Google Scholar 

  • —,J. F. Heremans, M. Th. Heremans, andH. G. Kunkel: Immunological studies of human gamma-globulin. Relation of the precipitates of whole gamma-globulin to those of the fragments produced by papain. J. Exp. Med.112, 203 (1960).

    PubMed  CAS  Google Scholar 

  • —,D. E. Olins, J. A. Gally, andN. D. Zinder: Reconstitution of immunologic activity by interaction of polypeptide chains of antibodies. Proc. Nat. Acad. Sci. (Wash.)50, 753 (1963).

    CAS  Google Scholar 

  • —, andM. D. Poulik: Studies on structural units of the γ-globulins. J. Exp. Med.113, 861 (1961).

    PubMed  CAS  Google Scholar 

  • Fahey, J. L.: The heterogeneity of γ-globulins. In: Advances in Immunology, edit.W. H. Taliaferro andJ. H. Humphrey, vol. 2, p. 42. New York and London: Academic Press (1962).

    Google Scholar 

  • —, andB. A. Askonas: Enzymatically produced subunits of proteins formed by plasma cells in mice. I. Gammaglobulin and gamma myeloma proteins. J. Exp. Med.115, 623 (1962).

    PubMed  CAS  Google Scholar 

  • —,W. S. Barth, R. D. Wochner, andT. A. Waldmann: Metabolism of human gamma-macroglobulins. J. clin. Invest.43, 1036 (1964).

    PubMed  Google Scholar 

  • —, andA. G. Robinson: Factors controlling the serum γ-globulin concentration. J. Exp. Med.118, 845 (1963).

    PubMed  CAS  Google Scholar 

  • Filitti-Wurmser, S., etL. Hartmann: Études physicochimiques des macroglobulines purifiées et des sérums humains normaux et pathologiques. Bull. Soc. Chim. biol. (Paris)54, 919 (1962).

    Google Scholar 

  • Fireman, P., W. E. Vannier, andH. C. Goodman: The association of skin-sensitizing antibody with the β2A-globulins in sera from ragweed-sensitive patients. J. Exp. Med.117, 603 (1963).

    PubMed  CAS  Google Scholar 

  • Fleischman, J. B., R. H. Pain, andR. R. Porter: Reduction of γ-globulins. Arch. Biochem., Suppl.1, 174 (1962).

    PubMed  Google Scholar 

  • —,R. R. Porter, andE. M. Press: The arrangement of the peptide chains in γ-globulin. Biochem. J.88, 220 (1963).

    PubMed  CAS  Google Scholar 

  • Franek, F.: Dissociation of animal 7 S γ-globulins by cleavage of disulfide bonds. Biochem. biophys. Res. Commun.4, 28 (1961).

    PubMed  CAS  Google Scholar 

  • Franek, F., O. Kotinek, L. Simek, andJ. Zikan: S-sulphonated anti-dinitrophenyl antibodies. Some specific features of the interaction between isolated H and L subunits. Internat. Symposium on the cellular and molecular basis of antibody formation, Prague 1964.

    Google Scholar 

  • —, andR. S. Nezlin: Recovery of antibody combining activity by interaction of different peptide chains isolated from purified horse antitoxins. Folia microbiol. (Praha)8, 128 (1963).

    CAS  Google Scholar 

  • Franklin, E. C.: Physicochemical and immunologic studies of low molecular γ-globulins of normal urine. J. clin. Invest.38, 2159 (1959).

    PubMed  CAS  Google Scholar 

  • —: Some properties of the breakdown products of human 7 S gamma-globulin and antibodies. J. clin. Invest.39, 986 (1960).

    Google Scholar 

  • —: The immune globulins. — Their structure and function and some techniques for their isolation. Progr. Allergy8, 58 (1964).

    CAS  Google Scholar 

  • Franklin, E. C., H. Fudenberg, M. Meltzer, andD. R. Stanworth: The structural basis for genetic variations of normal human γ-globulins. Proc. Nat. Acad. Sci. (Wash.)48, 914 (1962).

    CAS  Google Scholar 

  • —,M. Meltzer, F. Guggenheim, andJ. Lowenstein: An unusual micro γ-globulin in the serum and urine of a patient. Fed. Proc.22, 264 (1963).

    Google Scholar 

  • —, andD. R. Stanworth: Antigenic relationships between immune globulins and certain related paraproteins in man. J. Exp. Med.114, 521 (1961).

    PubMed  CAS  Google Scholar 

  • Fudenberg, H.: The hereditary human gamma-globulin (Gm) groups: Interpretations. Progr. Allergy7, 1 (1963).

    CAS  Google Scholar 

  • Fudenberg, H. H., G. Drews andA. Nisonoff: Serologic demonstration of dual specificity of rabbit bivalent hybrid antibody. J. Exp. Med.119, 151 (1964).

    PubMed  CAS  Google Scholar 

  • —, andA. Nisonoff: Properties of univalent 3.5 S fragments of 7 S agglutinating antibodies. J. clin. Invest.41, 1360 (1962).

    Google Scholar 

  • Gitlin, D., P. A. M. Gross, andC. A. Janeway: The gamma-globulins and their clinical significance. I. Chemistry, immunology and metabolism. New Engl. J. Med.260, 21 (1959).

    PubMed  CAS  Google Scholar 

  • —, andE. Merler: A comparison of the peptides released from rabbit antibodies by enzymatic hydrolysis. J. Exp. Med.114, 217 (1961).

    PubMed  CAS  Google Scholar 

  • Givol, D., andM. Sela: A comparison of fragments of rabbit antibodies and normal γ-globulin by the peptide-map technique. Biochemistry3, 451 (1964).

    PubMed  CAS  Google Scholar 

  • Grey, H. M.: Phylogeny of the immune response. J. Immunol.91, 819 (1963).

    PubMed  CAS  Google Scholar 

  • Grossberg, A. L., O. A. Roholt, andD. Pressman: Different distribution of antibodies of two specificities among γ-globulins of an individual rabbit. Biochemistry2, 989 (1963).

    PubMed  CAS  Google Scholar 

  • Grubb, R., andB. Swahn: Destruction of some agglutinins but not of others by two sulfhydryl compounds. Acta path. microbiol. scand.43, 305 (1958).

    PubMed  CAS  Google Scholar 

  • Gyenes, L., A. H. Sehon, S. O. Freedman, andZ. Ovary: The properties of fragments of skin-sensitizing and blocking antibodies as revealed by the Prausnitz-Kuestner, passive cutaneous anaphylaxis and hemagglutination reactions. Int. Arch. Allergy24, 106 (1964).

    PubMed  CAS  Google Scholar 

  • Habich, H., etA. Hässig: Essai d’analyse antigènique des paraprotéines dans la macroglobulinémie de Waldenstrøm. Vox Sang. (Basel)3, 99 (1953).

    Google Scholar 

  • Halpern, B. N., andO. L. Frick: Protection against foetal anaphylactic shock with γ-globulins in guinea pigs and mice. J. Immunol.88, 683 (1962).

    PubMed  CAS  Google Scholar 

  • Hanson, L. A.: Comparative immunological studies of the immune globulins of human milk and of blood serum. Int. Arch. Allergy18, 241 (1961).

    PubMed  CAS  Google Scholar 

  • Harboe, M., C. K. Osterland, andH. G. Kunkel: Localization of two genetic factors (Gm and Inv) to different areas of 7 S γ-globulin molecules. Science136, 979 (1962).

    PubMed  CAS  Google Scholar 

  • ——,K. M. Mannik, andH. G. Kunkel: Genetic characters of human γ-globulins and myeloma proteins. J. Exp. Med.116, 719 (1962).

    PubMed  CAS  Google Scholar 

  • Heremans, J. F., A. O. Carbonara, G. Mancini, andR. Lontie: Studies on normal and patholgoical γ1A-globulins and their subunits. In: Protides of the biological fluids, edit.H. Peeters. Amsterdam 1964.

    Google Scholar 

  • —, andJ. P. Vaerman: β2A-globulins as a possible carrier of allergic reaginic activity. Nature (Lond.)193, 1091 (1962).

    CAS  Google Scholar 

  • Hill, W. C.: Properties of purified horse macroglobulin antibodies. Thesis, University of Florida, Gainesville 1964.

    Google Scholar 

  • Hinz, C.: Personal communications 1958.

    Google Scholar 

  • Hitzig, W. H., andH. Isliker: Protides of the biological fluids. In: Proc. 7th Colloquium, edit.H. Peeters, p. 372,Bruges 1959.

    Google Scholar 

  • Hsiao S. H., andF. W. Putnam: The cleavage of human γ-globulin by papain. J. Biol. Chem.236, 122 (1961).

    PubMed  CAS  Google Scholar 

  • Iscaki, S., etM. Raynaud: Propriétés de fragments de molécules d’anticorps antitoxiques (antidiphtériques) obtenus par digestion pepsique du précipité spécifique et réduction. C. R. Acad. Sci. (Paris)253, 2286 (1961).

    Google Scholar 

  • Ishizaka, K.: Gamma-globulin and molecular mechanisms in hypersensitivity reactions. Progr. Allergy7, 32 (1963).

    CAS  Google Scholar 

  • —, andT. Ishizaka: Molecular basis of passive sensitization. II. The role of fragment III of γ-globulin and its disulfide bonds in passive sensitization and complement fixation. J. Immunol.93, 59 (1964).

    PubMed  CAS  Google Scholar 

  • Ishizaka, K., andT. Ishizaka, andM. Hathorn: Blocking of Prausnitz-Kuestner sensitization with reagin by “A chain” of human γA-globulin. Immunochem. 1964 (in press).

    Google Scholar 

  • Isliker, H. C.: The chemical nature of antibodies. Advanc. Protein Chem.12, 387 (1957).

    CAS  Google Scholar 

  • Isliker, H. C.: The properdin system and its significance in immunopathology. Immunopath. Ist. Internat. Symposium, p. 28, Basel 1958.

    Google Scholar 

  • —: Réactions non spécifiques de défense. Helv. med. Acta26, 634 (1959).

    PubMed  CAS  Google Scholar 

  • —: Les macroglobulines du plasma humain. Bull. Acad. suisse Sci. med.17, 139 (1961).

    CAS  Google Scholar 

  • Isliker, H. C., J. C. Cerottini, J. C. Jaton, andG. Magnenat: Fixation of specific and nonspecific plasma proteins in tumors. Internat. symposium on tumor chemotherapy, Lugano 1964.

    Google Scholar 

  • Isliker, H. C., H. Jacot-Guillarmod, andM. Thoeni: Reversible inactivation of γ1M-globulins. Anticomplementary activity and tissue affinity of human γ-globulin. NAS/NRC Symposium on gamma-globulin, Washington 1962.

    Google Scholar 

  • —,B. le Maire, andC. Morgan: The use of ferritin conjugated antibody-fragments in electron-microscopic studies of viruses. Path. et Microbiol. (Basel)27, 521 (1964).

    CAS  Google Scholar 

  • —, andE. Linder: Methods for the assay of properdin. Vox Sang. (Basel)3, 23 (1958).

    CAS  Google Scholar 

  • Isliker, H. C., andM. Thoeni: Unpublished data 1962.

    Google Scholar 

  • Jacot-Guillarmod, H.: Les macroglobulines sériques et leurs subunités; scission réversible et activité biologique. Thèse, Université de Lausanne 1964.

    Google Scholar 

  • —, etH. C. Isliker: Scission et réassociation des isoagglutinines traitées par des agents réducteurs des ponts disulfures. Préparation d’anticorps mixtes. Vox Sang. (Basel)7, 675 (1962).

    CAS  Google Scholar 

  • ——: Scission réversible des isoagglutinines 19 S. Étude de fixation des subunités. Vox Sang. (Basel)9, 31 (1964).

    CAS  Google Scholar 

  • Jaquet, H., B. Bloom, andJ. J. Cebra: The reductive dissociation of rabbit immune globulin in sodium dodecylsulfate. J. Immunol.92, 991 (1964).

    PubMed  CAS  Google Scholar 

  • Jaton, J. C., etH. C. Isliker: Étude de la fixation de fragments d’anticorps sur différents tissus. Helv. physiol. pharmacol. Acta20, C 62 (1962).

    Google Scholar 

  • Jaton, J. C., Scholer andIsliker: Unpublished data (1964).

    Google Scholar 

  • Kabat, E. A.: Heterogeneity in extent of the combining regions of human antidextran. J. Immunol.77, 377 (1956).

    PubMed  CAS  Google Scholar 

  • —: The upper limit of the size of the human antidextran combining site. J. Immunol.84, 82 (1960).

    PubMed  CAS  Google Scholar 

  • —, andM. M. Mayer: Purification of antibodies. In: Experimental Immunochemistry II. ed. Springfield: C. C. Thomas 1962.

    Google Scholar 

  • Kappeler, R., andH. C. Isliker: Unpublished data 1959.

    Google Scholar 

  • Karush, F.: Immunologic specificity and molecular structure. In: Advances in Immunology, vol. 2, p. 1. New York and London: Academic Press 1962.

    Google Scholar 

  • Karush, F.: Personal communication 1964.

    Google Scholar 

  • Keller, H., H. C. Isliker u.H. Aebi: Turnover des Properdins beim Kaninchen. Helv. physiol. pharmacol. Acta15, C 21 (1957).

    CAS  Google Scholar 

  • Killander, J., andP. Flodin: The fractionation of serum proteins by gel filtration. Vox Sang. (Basel)7, 113 (1962).

    Google Scholar 

  • Kjellén, L.: Reactions between adenovirus antigens and papain digested rabbit immune globulin. Arch. ges. Virusforsch.14, 189 (1964).

    PubMed  Google Scholar 

  • Kovacs, A. M., etM. Daune: Masse et dimensions d’une molécule de macroglobuline. Biochim. Biophys. Acta (Amst.)50, 249 (1961).

    CAS  Google Scholar 

  • Kunkel, H. C.: Macroglobulins and high molecular weight antibodies. In: The Plasma Proteins, vol. 1, p. 294, edit.F. W. Putnam. New York and London: Academic Press 1960.

    Google Scholar 

  • Landy, M., andL. Pillemer: Increased resistance to infection accompanying properdin alterations and following administration of bacterial lipopolysaccharides. J. Exp. Med.104, 383 (1956).

    PubMed  CAS  Google Scholar 

  • Leddy, J. P., G. L. Freeman, A. Luz, andR. H. Todd: Inactivation of the skin-sensitizing antibodies of human allergy by thiols. Proc. Soc. exp. Biol. (N.Y.)111, 7 (1962).

    CAS  Google Scholar 

  • Lepow, T.: Personal communication 1964.

    Google Scholar 

  • Mandy, W. J., M. M. Rivers, andA. Nisonoff: Recombination of univalent subunits derived from rabbit antibody. J. Biol. Chem.236, 3221 (1961).

    PubMed  CAS  Google Scholar 

  • Marler, E., C. A. Nelson, andC. Tanford: The polypeptide chains of rabbit γ-globulin and its papain-cleaved fragments. Biochemistry3, 279 (1964).

    PubMed  CAS  Google Scholar 

  • McDougall, E. I., andH. F. Deutsch: A comparison of the native and monomer forms of macroglobulin from pathological human serum with particular reference to electrophoretic mobility differences. Biochem. J.90, 163 (1964).

    PubMed  CAS  Google Scholar 

  • ——: Disulfide bonds in macroglobulin: A correction of interpretations of results. Biochem. J.92, 1c (1964).

    Google Scholar 

  • McFadden, M. L., andE. L. Smith: Free amino groups and N-terminal sequence of rabbit antibodies. J. Biol. Chem.214, 185 (1955).

    PubMed  CAS  Google Scholar 

  • Metzger, H., L. Wofsy, andS. J. Singer: A specific antibody-hapten reaction with novel spectral properties. Arch. Biochem.103, 206 (1963).

    PubMed  CAS  Google Scholar 

  • ———: Affinity labelling of the active sites of antibodies to the 2,4-dinitrophenyl hapten. Biochemistry2, 979 (1963).

    PubMed  CAS  Google Scholar 

  • ———: The participation of A and B polypeptide chains in the active sites of antibody molecules. Proc. Nat. Acad. Sci. (Wash.)51, 612 (1964).

    CAS  Google Scholar 

  • Micheli, A., H. Jacot-Guillarmod etH. C.Isliker: Essai de scission des liaisons disulfures protéiques à l’aide d’un système enzymatique. Helv. physiol. pharmacol. Acta21, 38 (1963).

    Google Scholar 

  • Miescher, P. A., H. L. Spiegelberg, andB. Benacerraf: Mechanism of elimination of sensitized rat erythrocytes and E. Coli from the circulation of mice. In: Immunopathology, IIIrd Internat. Symposium, La Jolla, Calif. USA; edit.P. Grabar, andP. A. Miescher. Basel: Benno Schwabe & Co. 1963.

    Google Scholar 

  • Molinaro, G., J. C. Jaton, H. J. Scholer, andH. C. Isliker: Int. Arch. Allergy (in press).

    Google Scholar 

  • Nelson, R. A.: An alternative mechanism for the properdin system. J. Exp. Med.108, 515 (1958).

    PubMed  CAS  Google Scholar 

  • Nisonoff, A., G. Markus, andF. C. Wissler: Separation of univalent fragments of rabbit antibody by reduction of a single labile disulfide bond. Nature (Lond.)189, 293 (1961).

    CAS  Google Scholar 

  • —, andJ. L. Palmer: Hybridization of half molecules of rabbit γ-globulin. Science143, 222 (1964).

    Google Scholar 

  • —, andM. M. Rivers: Recombination of a mixture of univalent antibody fragments of different specificity. Arch. Biochem.93, 460 (1961).

    PubMed  CAS  Google Scholar 

  • F. C. Wissler, L. N. Lipman, andD. L. Woernley: Separation of univalent fragments from the bivalent rabbit antibody molecule by reduction of disulfide bond. Arch. Biochem.89, 230 (1960).

    PubMed  CAS  Google Scholar 

  • ——, andD. L. Woernley: Mechanism of formation of univalent fragments of rabbit antibody. Biochem. Biophys. Res. Commun.1, 318 (1959).

    CAS  Google Scholar 

  • Nolan, C., andE. L. Smith: Glycopeptides. II. Isolation and properties of glycopeptides from rabbit γ-globulin. J. Biol. Chem.237, 446 (1962).

    PubMed  CAS  Google Scholar 

  • Nussenzweig, R. S., C. Merryman, andB. Benacerraf: Electrophoretic separation and properties of mouse antihapten antibodies involved in passive cutaneous anaphylaxis and passive hemolysis. J. Exp. Med.120, 315 (1964).

    PubMed  CAS  Google Scholar 

  • Olesen, H.: Turnover studies with iodine labeled gamma-macroglobulin and albumin. Scand. J. Clin. Lab. Invest.15, 497 (1963).

    PubMed  CAS  Google Scholar 

  • Oncley, J. L., M. Melin, D. A. Richert, J. W. Cameron, andP. M. Gross: The separation of the antibodies, isoagglutinins, prothrombin, plasminogen, and β1-lipoprotein into subfractions of human plasma. J. Amer. Chem. Soc.71, 541 (1949).

    CAS  Google Scholar 

  • Ovary, Z., B. Benacerraf, andK. J. Bloch: Properties of guinea pig 7 S antibodies. II. Identification of antibodies involved in passive cutaneous and systemic anaphylaxis. J. Exp. Med.117, 951 (1963).

    PubMed  CAS  Google Scholar 

  • Ovary, Z., K. J. Bloch, andB. Benacerraf: Unpublished data.

    Google Scholar 

  • —, andF. Karush: Studies on the immunologic mechanism of anaphylaxis. II. Sensitizing and combining capacityin vivo of fractions separated from papain digests of antihapten antibody. J. Immunol.86, 146 (1961).

    PubMed  CAS  Google Scholar 

  • —, andA. Taranta: Passive cutaneous anaphylaxis with antibody fragments. Science140, 193 (1963).

    PubMed  CAS  Google Scholar 

  • Pain, R. H.: The molecular weights of the peptide chains of γ-globulins. Biochem. J.88, 234 (1963).

    PubMed  CAS  Google Scholar 

  • Palmer, J. L., W. J. Mandy, andA. Nisonoff: Heterogeneity of rabbit antibody and its subunits. Proc. Nat. Acad. Sci. (Wash.)48, 49 (1962).

    CAS  Google Scholar 

  • —, andA. Nisonoff: Dissociation of rabbit γ-globulin into half-molecules after reduction of one labile disulfide bond. Biochemistry3, 863 (1964).

    PubMed  CAS  Google Scholar 

  • Parke, J. A. C., andP. J. Avis: The effect of digestion with papain and pepsin upon the antitoxin activity of rabbit antibody. Immunology7, 248 (1964).

    PubMed  CAS  Google Scholar 

  • Petermann, M. L.: The splitting of human γ-globulin antibodies by papain and bromelin. J. Amer. Chem. Soc.68, 106 (1946).

    CAS  Google Scholar 

  • Pillemer, L., L. Blum, I. H. Lepow, O. A. Ross, E. W. Todd, andA. C. Wardlaw: The properdin system and immunity: I. Demonstration and isolation of a new serum protein, properdin, and its role in immune phenomena. Science120, 279 (1954).

    PubMed  CAS  Google Scholar 

  • Porter, R. R.: A chemical study of rabbit antiovalbumin. Biochem. J.46, 473 (1950).

    PubMed  CAS  Google Scholar 

  • —: The hydrolysis of rabbit gamma-globulin and antibodies with crystalline papain. Biochem. J.73, 119 (1959).

    PubMed  CAS  Google Scholar 

  • —: Chemical structure of γ-globulin and antibodies. Brit. med. Bull.19, 197 (1963).

    PubMed  CAS  Google Scholar 

  • Putnam, F. W., M. Tan, L. T. Lynn, C. W. Easley, andS. Migita: The cleavage of rabbit γ-globulin by papain. J. Biol. Chem.237, 717 (1962).

    PubMed  CAS  Google Scholar 

  • Raynaud, M., andS. Iscaki: Co-precipitating properties of 3S fragments derived from horse antitoxins. Nature (Lond.)203, 758 (1964).

    CAS  Google Scholar 

  • Reisner, C. A., andE. C. Franklin: Studies of mercaptoethanol-dissociated normal human 19S γ-globulin and pathologic macroglobulins from patients with macroglobulinemia. J. Immunol.87, 654 (1961).

    PubMed  CAS  Google Scholar 

  • Reiss, A. M., andO. J. Plescia: Fixation of complement to fragments of antibody. Science141, 812 (1963).

    PubMed  CAS  Google Scholar 

  • Ritzmann, S. E., S. N. Coleman, andW. C. Lewin: The effect of some mercaptans upon macrocryoglobulin; modifications induced by cysteamine, penicillamine and penicillin. J. clin. Invest.39, 1320 (1960).

    PubMed  CAS  Google Scholar 

  • Rockey, J. H., andH. G. Kunkel: Unusual sedimentation and sulfhydryl sensitivity of certain isohemagglutinins and skin-sensitizing antibody. Proc. Soc. exp. Biol. (N.Y.)110, 101 (1962).

    CAS  Google Scholar 

  • Roholt, O., K. Onoue, andD. Pressman: Specific combination of H and L chains of rabbit γ-globulins. Proc. Nat. Acad. Sci. (Wash.)51, 173 (1964).

    CAS  Google Scholar 

  • —,G. Radzimski, andD. Pressman: Antibody-combining site: the B polypeptide chain. Science141, 726 (1963).

    PubMed  CAS  Google Scholar 

  • Rosevear, J. W., andE. L. Smith: Glycopeptides. I. Isolation and properties of glycopeptides from a fraction of human γ-globulin. J. Biol. Chem.236, 425 (1961).

    PubMed  CAS  Google Scholar 

  • Rothstein, F.: Thesis, Harvard University, Boston 1962.

    Google Scholar 

  • Rowley, D.: Le système properdine et son rôle dans l’immunité. Triangle (Sandoz, Basel)3, 17 (1957).

    CAS  Google Scholar 

  • Rowley, D., H. Isliker, andM. Thoeni: Nature (in press).

    Google Scholar 

  • —, andK. J. Turner: Increase in macroglobulin antibodies of mouse and pig following injection of bacterial lipopolysaccharide. Immunology7, 394 (1964).

    PubMed  CAS  Google Scholar 

  • Rytel, M. W.: Properdin. Science130, 826 (1959).

    PubMed  CAS  Google Scholar 

  • Schultze, H. E., H. Haupt, K. Heide, N. Heimburger, andG. Schwick: Comparative investigations on purified diphtheria and tetanus T-components and their fragments. Personal communication 1964.

    Google Scholar 

  • ———,G. Möschlin, R. Schmidtberger u.G. Schwick: Untersuchungen über Gamma-Makroglobuline des menschlichen Serums. Z. Naturforsch.17B, 313 (1962).

    Google Scholar 

  • —, u.G. Schwick: Neue Möglichkeiten intravenöser Gamma-globulin Applikationen. Dtsch. med. Wschr.87, 1643 (1962).

    PubMed  CAS  Google Scholar 

  • Schur, P. H., andE. L. Becker: Pepsin digestion of rabbit and sheep antibodies. The effect on complement fixation. J. Exp. Med.118, 891 (1963).

    PubMed  CAS  Google Scholar 

  • Sehon, A. H.: The nature of antibodies in conditions of hypersensitivity in man. In: Protides of the biological fluids, p. 67, edit.H. Peeters. Amsterdam 1964.

    Google Scholar 

  • Silman, H. I., J. J. Cebra, andD. Givol: The carboxyl terminal amino acids of rabbit γ-globulin. J. Biol. Chem.237, 2196 (1962).

    PubMed  CAS  Google Scholar 

  • Singer, S. J., andA. F. Schick: The properties of specific stains for electron microscopy. J. biophys. biochem. Cytol.9, 519 (1961).

    PubMed  CAS  Google Scholar 

  • Singer, S. J., L. Wofsy, andA. H. Good: Studies of antibody combining sites by affinity labelling. Internat. Symposium on the cellular and molecular basis of antibody formation, Prague 1964.

    Google Scholar 

  • Sober, H. A., F. J. Gutter, M. M. Wycoff, andE. A. Peterson: Chromatography of proteins. II. Fractionation of serum proteins on anion exchanger cellulose. J. Amer. Chem. Soc.78, 756 (1956).

    CAS  Google Scholar 

  • Sorkin, E.: “Cytophilic antibody”. The immunologically competent cell: A Ciba Foundation Symposium. Ed. byG. E. W. Wolstenholme andM. P. Cameren, p. 53. London: Churchill 1963.

    Google Scholar 

  • Spiegelberg, H. L., andW. O. Weigle: The catabolism of homologous and heterologous 7S γ-globulin fragments. In press, 1965.

    Google Scholar 

  • Stelos, P., O. Roholt, andD. Pressman: Heterogeneity of the major fractions of papain digests of rabbit antibody. J. Immunol.89, 113 (1962).

    PubMed  CAS  Google Scholar 

  • Strauss, A. J. L., P. G. Kemp, W. E. Vannier, andH. C. Goodman: Purification of human serum γ-globulin for immunologic studies: γ-globulin fragmentation after sulfate precipitation and prolonged dialysis. J. Immunol.93, 24 (1964).

    PubMed  CAS  Google Scholar 

  • Svehag, S. E. andB. Mandel: The formation and properties of poliovirus-neutralizing antibody. J. Exp. Med.119, 1 (1964).

    PubMed  CAS  Google Scholar 

  • Terr, A. I., andJ. D. Bentz: Density-gradient sedimentation of skin-sensitizing antibody and γ2A-globulin in serum of allergic individuals. Proc. Soc. exp. Biol. (N.Y.)115, 721 (1964).

    CAS  Google Scholar 

  • Thorbecke, G. J., B. Benacerraf, andZ. Ovary: Antigenic relationship between two types of 7S guinea pig γ-globulins. J. Immunol.91, 670 (1963).

    PubMed  CAS  Google Scholar 

  • Uhr, J. W., andM. S. Finkelstein: Antibody formation. IV. Formation of rapidly and slowly sedimenting antibodies and immunological memory to bacteriophage. J. Exp. Med.117, 457 (1963).

    PubMed  CAS  Google Scholar 

  • Weil, A. J., J. A. Parfentiev, andK. L. Bowmann: Antigenic qualities of antitoxins. J. Immunol.35, 399 (1938).

    Google Scholar 

  • Wiedermann, G., P. A. Miescher, andE. C. Franklin: Effect of mercaptoethanol on complement binding ability of human 7S gammaglobulin. Proc. Soc. exp. Biol. (N.Y.)113, 609 (1963).

    CAS  Google Scholar 

  • Wilbrandt, R.: Beitrag zum Mechanismus der reduktiven Spaltung von Makroglobulinen. Thesis, University of Berne 1963.

    Google Scholar 

Download references

Authors

Rights and permissions

Reprints and permissions

Copyright information

© 1965 Springer-Verlag

About this paper

Cite this paper

Isliker, H., Jacot-Guillarmod, H., Jaton, J.C. (1965). The structure and biological activity of immunoglobulins and their subunits. In: Ergebnisse der physiologie biologischen chemie und experimentellen pharmakologie. Ergebnisse der Physiologie, biologischen Chemie und experimentellen Pharmakologie, vol 56. Springer, Berlin, Heidelberg. https://doi.org/10.1007/BFb0117429

Download citation

  • DOI: https://doi.org/10.1007/BFb0117429

  • Published:

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-540-03285-4

  • Online ISBN: 978-3-540-37128-1

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics