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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).
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).
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.
—,P. Kistler, F. Jeunet, andH. Isliker: Intravenous administration of γ-globulin. Vox Sang. (Basel)7, 157 (1962).
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).
Binaghi, R. A., andB. Benacerraf: Properties of rat anaphylactic antibody. J. Immunol. (in press) (1964).
——,K. J. Bloch, andF. M. Kourilsky: Properties of rat anaphylactic antibody. J. Immunol.92, 927 (1964).
—,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).
Blanc, B.: Les protéines du lactosérum. Leurs relations avec l'immunité et le métabolisme du fer. Thèse, Université de Lausanne 1962.
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).
Boyden, S. V.: Cytophilic antibody in guinea-pigs with delayed-type hypersensitivity. Immunology7, 474 (1964).
—, andE. Sorkin: The absorption of antibody and antigen by spleen cells in vitro. Some further experiments. Immunology4, 244 (1961).
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).
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.
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).
Cerottini, J., J. C. Jaton, T. Froidevaux, etH. Isliker: Immunofluorescence à l'aide de fragments d'anticorps. Helv. physiol. pharmacol. Acta22, C9 (1964).
Cohen, S.: Properties of the separated chains of human γ-globulin. Nature (Lond.)197, 253 (1963).
—, andT. Freeman: Metabolic heterogeneity of human gamma-globulins. Biochem. J.76, 475 (1960).
— andR. R. Porter: Heterogeneity of the peptide chains of γ-globulin. Biochem. J.90, 278 (1964).
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).
Deutsch, H. F., andJ. I. Morton: Dissociation of human serum macroglobulins. Science125, 600 (1957).
——: Human serum macroglobulins and dissociation units. J. Biol. Chem.231, 1107 (1958).
—,E. R. Stiehm, andJ. I. Morton: Action of papain on human serum globulins. J. Biol. Chem.236, 2216 (1961).
Dixon, F.: The lack of absorption of ingested bovine antibody in humans. J. Immunol.83, 437 (1959).
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.
—, andB. Benacerraf: On structural and functional relations between antibodies and gamma-globulins. Proc. Nat. Acad. Sci. (Wash.)48, 1035 (1962).
—, 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).
——: A model for the 7S antibody molecule. Proc. Nat. Acad. Sci. (Wash.)51, 846 (1964).
—,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).
—,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).
—, andM. D. Poulik: Studies on structural units of the γ-globulins. J. Exp. Med.113, 861 (1961).
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).
—, 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).
—,W. S. Barth, R. D. Wochner, andT. A. Waldmann: Metabolism of human gamma-macroglobulins. J. clin. Invest.43, 1036 (1964).
—, andA. G. Robinson: Factors controlling the serum γ-globulin concentration. J. Exp. Med.118, 845 (1963).
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).
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).
Fleischman, J. B., R. H. Pain, andR. R. Porter: Reduction of γ-globulins. Arch. Biochem., Suppl.1, 174 (1962).
—,R. R. Porter, andE. M. Press: The arrangement of the peptide chains in γ-globulin. Biochem. J.88, 220 (1963).
Franek, F.: Dissociation of animal 7 S γ-globulins by cleavage of disulfide bonds. Biochem. biophys. Res. Commun.4, 28 (1961).
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.
—, 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).
Franklin, E. C.: Physicochemical and immunologic studies of low molecular γ-globulins of normal urine. J. clin. Invest.38, 2159 (1959).
—: Some properties of the breakdown products of human 7 S gamma-globulin and antibodies. J. clin. Invest.39, 986 (1960).
—: The immune globulins. — Their structure and function and some techniques for their isolation. Progr. Allergy8, 58 (1964).
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).
—,M. Meltzer, F. Guggenheim, andJ. Lowenstein: An unusual micro γ-globulin in the serum and urine of a patient. Fed. Proc.22, 264 (1963).
—, andD. R. Stanworth: Antigenic relationships between immune globulins and certain related paraproteins in man. J. Exp. Med.114, 521 (1961).
Fudenberg, H.: The hereditary human gamma-globulin (Gm) groups: Interpretations. Progr. Allergy7, 1 (1963).
Fudenberg, H. H., G. Drews andA. Nisonoff: Serologic demonstration of dual specificity of rabbit bivalent hybrid antibody. J. Exp. Med.119, 151 (1964).
—, andA. Nisonoff: Properties of univalent 3.5 S fragments of 7 S agglutinating antibodies. J. clin. Invest.41, 1360 (1962).
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).
—, andE. Merler: A comparison of the peptides released from rabbit antibodies by enzymatic hydrolysis. J. Exp. Med.114, 217 (1961).
Givol, D., andM. Sela: A comparison of fragments of rabbit antibodies and normal γ-globulin by the peptide-map technique. Biochemistry3, 451 (1964).
Grey, H. M.: Phylogeny of the immune response. J. Immunol.91, 819 (1963).
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).
Grubb, R., andB. Swahn: Destruction of some agglutinins but not of others by two sulfhydryl compounds. Acta path. microbiol. scand.43, 305 (1958).
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).
Habich, H., etA. Hässig: Essai d'analyse antigènique des paraprotéines dans la macroglobulinémie de Waldenstrøm. Vox Sang. (Basel)3, 99 (1953).
Halpern, B. N., andO. L. Frick: Protection against foetal anaphylactic shock with γ-globulins in guinea pigs and mice. J. Immunol.88, 683 (1962).
Hanson, L. A.: Comparative immunological studies of the immune globulins of human milk and of blood serum. Int. Arch. Allergy18, 241 (1961).
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).
——,K. M. Mannik, andH. G. Kunkel: Genetic characters of human γ-globulins and myeloma proteins. J. Exp. Med.116, 719 (1962).
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.
—, andJ. P. Vaerman: β2A-globulins as a possible carrier of allergic reaginic activity. Nature (Lond.)193, 1091 (1962).
Hill, W. C.: Properties of purified horse macroglobulin antibodies. Thesis, University of Florida, Gainesville 1964.
Hinz, C.: Personal communications 1958.
Hitzig, W. H., andH. Isliker: Protides of the biological fluids. In: Proc. 7th Colloquium, edit.H. Peeters, p. 372,Bruges 1959.
Hsiao S. H., andF. W. Putnam: The cleavage of human γ-globulin by papain. J. Biol. Chem.236, 122 (1961).
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).
Ishizaka, K.: Gamma-globulin and molecular mechanisms in hypersensitivity reactions. Progr. Allergy7, 32 (1963).
—, 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).
Ishizaka, K., andT. Ishizaka, andM. Hathorn: Blocking of Prausnitz-Kuestner sensitization with reagin by “A chain” of human γA-globulin. Immunochem. 1964 (in press).
Isliker, H. C.: The chemical nature of antibodies. Advanc. Protein Chem.12, 387 (1957).
Isliker, H. C.: The properdin system and its significance in immunopathology. Immunopath. Ist. Internat. Symposium, p. 28, Basel 1958.
—: Réactions non spécifiques de défense. Helv. med. Acta26, 634 (1959).
—: Les macroglobulines du plasma humain. Bull. Acad. suisse Sci. med.17, 139 (1961).
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.
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.
—,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).
—, andE. Linder: Methods for the assay of properdin. Vox Sang. (Basel)3, 23 (1958).
Isliker, H. C., andM. Thoeni: Unpublished data 1962.
Jacot-Guillarmod, H.: Les macroglobulines sériques et leurs subunités; scission réversible et activité biologique. Thèse, Université de Lausanne 1964.
—, 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).
——: Scission réversible des isoagglutinines 19 S. Étude de fixation des subunités. Vox Sang. (Basel)9, 31 (1964).
Jaquet, H., B. Bloom, andJ. J. Cebra: The reductive dissociation of rabbit immune globulin in sodium dodecylsulfate. J. Immunol.92, 991 (1964).
Jaton, J. C., etH. C. Isliker: Étude de la fixation de fragments d'anticorps sur différents tissus. Helv. physiol. pharmacol. Acta20, C 62 (1962).
Jaton, J. C., Scholer andIsliker: Unpublished data (1964).
Kabat, E. A.: Heterogeneity in extent of the combining regions of human antidextran. J. Immunol.77, 377 (1956).
—: The upper limit of the size of the human antidextran combining site. J. Immunol.84, 82 (1960).
—, andM. M. Mayer: Purification of antibodies. In: Experimental Immunochemistry II. ed. Springfield: C. C. Thomas 1962.
Kappeler, R., andH. C. Isliker: Unpublished data 1959.
Karush, F.: Immunologic specificity and molecular structure. In: Advances in Immunology, vol. 2, p. 1. New York and London: Academic Press 1962.
Karush, F.: Personal communication 1964.
Keller, H., H. C. Isliker u.H. Aebi: Turnover des Properdins beim Kaninchen. Helv. physiol. pharmacol. Acta15, C 21 (1957).
Killander, J., andP. Flodin: The fractionation of serum proteins by gel filtration. Vox Sang. (Basel)7, 113 (1962).
Kjellén, L.: Reactions between adenovirus antigens and papain digested rabbit immune globulin. Arch. ges. Virusforsch.14, 189 (1964).
Kovacs, A. M., etM. Daune: Masse et dimensions d'une molécule de macroglobuline. Biochim. Biophys. Acta (Amst.)50, 249 (1961).
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.
Landy, M., andL. Pillemer: Increased resistance to infection accompanying properdin alterations and following administration of bacterial lipopolysaccharides. J. Exp. Med.104, 383 (1956).
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).
Lepow, T.: Personal communication 1964.
Mandy, W. J., M. M. Rivers, andA. Nisonoff: Recombination of univalent subunits derived from rabbit antibody. J. Biol. Chem.236, 3221 (1961).
Marler, E., C. A. Nelson, andC. Tanford: The polypeptide chains of rabbit γ-globulin and its papain-cleaved fragments. Biochemistry3, 279 (1964).
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).
——: Disulfide bonds in macroglobulin: A correction of interpretations of results. Biochem. J.92, 1c (1964).
McFadden, M. L., andE. L. Smith: Free amino groups and N-terminal sequence of rabbit antibodies. J. Biol. Chem.214, 185 (1955).
Metzger, H., L. Wofsy, andS. J. Singer: A specific antibody-hapten reaction with novel spectral properties. Arch. Biochem.103, 206 (1963).
———: Affinity labelling of the active sites of antibodies to the 2,4-dinitrophenyl hapten. Biochemistry2, 979 (1963).
———: The participation of A and B polypeptide chains in the active sites of antibody molecules. Proc. Nat. Acad. Sci. (Wash.)51, 612 (1964).
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).
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.
Molinaro, G., J. C. Jaton, H. J. Scholer, andH. C. Isliker: Int. Arch. Allergy (in press).
Nelson, R. A.: An alternative mechanism for the properdin system. J. Exp. Med.108, 515 (1958).
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).
—, andJ. L. Palmer: Hybridization of half molecules of rabbit γ-globulin. Science143, 222 (1964).
—, andM. M. Rivers: Recombination of a mixture of univalent antibody fragments of different specificity. Arch. Biochem.93, 460 (1961).
—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).
——, andD. L. Woernley: Mechanism of formation of univalent fragments of rabbit antibody. Biochem. Biophys. Res. Commun.1, 318 (1959).
Nolan, C., andE. L. Smith: Glycopeptides. II. Isolation and properties of glycopeptides from rabbit γ-globulin. J. Biol. Chem.237, 446 (1962).
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).
Olesen, H.: Turnover studies with iodine labeled gamma-macroglobulin and albumin. Scand. J. Clin. Lab. Invest.15, 497 (1963).
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).
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).
Ovary, Z., K. J. Bloch, andB. Benacerraf: Unpublished data.
—, 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).
—, andA. Taranta: Passive cutaneous anaphylaxis with antibody fragments. Science140, 193 (1963).
Pain, R. H.: The molecular weights of the peptide chains of γ-globulins. Biochem. J.88, 234 (1963).
Palmer, J. L., W. J. Mandy, andA. Nisonoff: Heterogeneity of rabbit antibody and its subunits. Proc. Nat. Acad. Sci. (Wash.)48, 49 (1962).
—, andA. Nisonoff: Dissociation of rabbit γ-globulin into half-molecules after reduction of one labile disulfide bond. Biochemistry3, 863 (1964).
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).
Petermann, M. L.: The splitting of human γ-globulin antibodies by papain and bromelin. J. Amer. Chem. Soc.68, 106 (1946).
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).
Porter, R. R.: A chemical study of rabbit antiovalbumin. Biochem. J.46, 473 (1950).
—: The hydrolysis of rabbit gamma-globulin and antibodies with crystalline papain. Biochem. J.73, 119 (1959).
—: Chemical structure of γ-globulin and antibodies. Brit. med. Bull.19, 197 (1963).
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).
Raynaud, M., andS. Iscaki: Co-precipitating properties of 3S fragments derived from horse antitoxins. Nature (Lond.)203, 758 (1964).
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).
Reiss, A. M., andO. J. Plescia: Fixation of complement to fragments of antibody. Science141, 812 (1963).
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).
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).
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).
—,G. Radzimski, andD. Pressman: Antibody-combining site: the B polypeptide chain. Science141, 726 (1963).
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).
Rothstein, F.: Thesis, Harvard University, Boston 1962.
Rowley, D.: Le système properdine et son rôle dans l'immunité. Triangle (Sandoz, Basel)3, 17 (1957).
Rowley, D., H. Isliker, andM. Thoeni: Nature (in press).
—, andK. J. Turner: Increase in macroglobulin antibodies of mouse and pig following injection of bacterial lipopolysaccharide. Immunology7, 394 (1964).
Rytel, M. W.: Properdin. Science130, 826 (1959).
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.
———,G. Möschlin, R. Schmidtberger u.G. Schwick: Untersuchungen über Gamma-Makroglobuline des menschlichen Serums. Z. Naturforsch.17B, 313 (1962).
—, u.G. Schwick: Neue Möglichkeiten intravenöser Gamma-globulin Applikationen. Dtsch. med. Wschr.87, 1643 (1962).
Schur, P. H., andE. L. Becker: Pepsin digestion of rabbit and sheep antibodies. The effect on complement fixation. J. Exp. Med.118, 891 (1963).
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.
Silman, H. I., J. J. Cebra, andD. Givol: The carboxyl terminal amino acids of rabbit γ-globulin. J. Biol. Chem.237, 2196 (1962).
Singer, S. J., andA. F. Schick: The properties of specific stains for electron microscopy. J. biophys. biochem. Cytol.9, 519 (1961).
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.
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).
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.
Spiegelberg, H. L., andW. O. Weigle: The catabolism of homologous and heterologous 7S γ-globulin fragments. In press, 1965.
Stelos, P., O. Roholt, andD. Pressman: Heterogeneity of the major fractions of papain digests of rabbit antibody. J. Immunol.89, 113 (1962).
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).
Svehag, S. E. andB. Mandel: The formation and properties of poliovirus-neutralizing antibody. J. Exp. Med.119, 1 (1964).
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).
Thorbecke, G. J., B. Benacerraf, andZ. Ovary: Antigenic relationship between two types of 7S guinea pig γ-globulins. J. Immunol.91, 670 (1963).
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).
Weil, A. J., J. A. Parfentiev, andK. L. Bowmann: Antigenic qualities of antitoxins. J. Immunol.35, 399 (1938).
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).
Wilbrandt, R.: Beitrag zum Mechanismus der reduktiven Spaltung von Makroglobulinen. Thesis, University of Berne 1963.
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From the Institute of Biochemistry, University of Lausanne, and the Swiss Institute for Experimental Cancer Research, Lausanne, Switzerland.
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Isliker, H., Jacot-Guillarmod, H. & Jaton, J.C. The structure and biological activity of immunoglobulins and their subunits. Ergebnisse der Physiologie und exper. Pharmakologie 56, 67–113 (1965). https://doi.org/10.1007/BF02270549
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DOI: https://doi.org/10.1007/BF02270549