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Structure and Formation of Antibodies

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Current Problems in Immunology

Part of the book series: Bayer-Symposium ((BAYER-SYMP,volume 1))

Abstract

Antibodies are proteins which are produced in vertebrates after stimulation with an antigen. They are specifically directed against the antigen which has caused their production.

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References

  • Appella, E., and D. Ein: Two types of lambda polypeptide chains in human immunoglobuline based on an amino acid substitution at position 190. Proc. nat. Acad. Sci. (Wash.) 57, 1449 (1967).

    Article  CAS  Google Scholar 

  • Attardi, G. P., P. C. Huang, and S. Kabat: Recognition of ribosomal RNA sites in DNA. 1. Analysis of the E. coli system. Proc. nat. Acad. Sci. (Wash.) 58, 1490 (1965).

    Article  Google Scholar 

  • Baglioni, C.: The fusion of two peptide chains in hemoglobin Lepore and its interpretation as a genetic deletion. Proc. nat. Acad. Sci. (Wash.) 48, 1880 (1962).

    Article  CAS  Google Scholar 

  • Baglioni, C.Homologies in the position of cysteine residues of K and L-type chains of human immunoglobulins. Biochem. biophys. Res. Commun. 26, 82 (1967).

    Google Scholar 

  • Baglioni, C., L. Alescio-Zonta, D. Cioli, and A. Carbonara: Allelic antigenic factor Inv(a) of the light chains of human immunoglobulins• chemical basis. Science 152, 1519 (1966).

    Article  Google Scholar 

  • Becker, M. J., and A. Rich: Polyribosomes of tissues producing antibodies. Nature (Lond.) 212, 142 (1966).

    Article  CAS  Google Scholar 

  • Borst, P., G. Ruttenberg, and A. M. Kroon: Mitochondrial DNA. II Sedimentation analysis and electron microscopy of mitochondrial DNA from chick liver. Biochim. biophys. Acta (Amst.) 149, 156 (1967).

    Article  CAS  Google Scholar 

  • Braunitzer, G.: Die Primärstruktur der Eiweißstoffe. Naturwissenschaften 54, 407 (1967).

    Article  PubMed  CAS  Google Scholar 

  • Braunitzer, G., K. Hilse, V. Rudloff, and N. Hilschmann• The hemoglobins. Advanc. Protein Chem. 19, 1 (1964).

    Article  CAS  Google Scholar 

  • Britten, R. J., and D. E. Kohne: Repeated sequences in DNA. Science 161, 529 (1968).

    Article  PubMed  CAS  Google Scholar 

  • Cebra, J. J., J. E. Colberg, and S. Dray: Rabbit lymphoid cells differentiated with respect to a-, y-, and ii-heavy polypeptide chains and to allotypic markers AA1 and AA2. J. exp. Med. 123, 547 (1966).

    Article  PubMed  CAS  Google Scholar 

  • Cohen, S., and C. Milstein: Structure and biological properties of immunoglobuline. Advanc. Immunol. 7, 1 (1967).

    Article  CAS  Google Scholar 

  • Cunningham, B. A., P. D. Gottlieb, W. H. Konigsberg, and G. M. Edelman: The covalent structure of a human yG-immunoglobulin. V. Partial amino acid sequence of the light chain. Biochemistry 7, 1983 (1968).

    Google Scholar 

  • Hill, R. L., R. Delaney, R. E. Fellows, Jr., and H. E. Lebovitz: The evolutionary origins of the immunoglobulins. Proc. nat. Acad. Sci. (Wash.) 56, 1762 (1966).

    Article  CAS  Google Scholar 

  • Dreyer, W. J., and J. C. Bennett: The molecular basis of antibody formation: a paradox. Proc. nat. Acad. Sci. (Wash.) 54, 864 (1965).

    Article  CAS  Google Scholar 

  • Dreyer, W. J., and J. C. Bennett, W. R. Gray, and L. Hood: The genetic, molecular and cellular basis of antibody formation: some facts and a unifying hypothesis. Cold Spr. Barb. Symp. quant. Biol. 32, 353 (1967).

    CAS  Google Scholar 

  • Edelman, G. M., and J. A. Gaily: The nature of Bence-Jones proteins. J. exp. Med. 116, 207 (1962).

    Article  PubMed  CAS  Google Scholar 

  • Edelman, G. M., and J. A. Gaily: A model for the 7s antibody molecule. Proc. nat. Acad. Sci. (Wash.) 51, 846 (1964).

    Article  CAS  Google Scholar 

  • Edelman, G. M., and J. A. Gaily: Somatic recombination of duplicated genes: an hypothesis on the origin of antibody diversity. Proc. nat. Acad. Sci. (Wash.) 57, 353 (1967).

    Article  CAS  Google Scholar 

  • Ein, D.: Nonallelic behaviour of the Oz groups in human lambda immunoglobulin chains. Proc. nat. Acad. Sci. (Wash.) 60, 982 (1968).

    Article  CAS  Google Scholar 

  • Ein, D., and J. L. Fahey: Two types of lambda polypeptide chains in human immunoglobulins. Science 156, 947 (1967).

    Article  PubMed  CAS  Google Scholar 

  • Fleischman, J. B., R. R. Porter, and E. M. Press: The arrangement of the peptide chains in y-globulin. Biochem. J. 88, 220 (1963).

    PubMed  CAS  Google Scholar 

  • Frangione, B., and C. Milstein: Disulphide bridges of immunoglobulin G1 heavy chains. Nature (Lond.) 216, 939 (1967).

    Article  CAS  Google Scholar 

  • Good, R. A., and B. W. Papermaster: Ontogeny and phylogeny of adaptive immunity. Advanc. Immunol. 4, 1 (1964).

    Article  Google Scholar 

  • Gottlieb, P. D., B. A. Cunningham, M. J. Waxdal, W. H. Konigsberg, and G. M. Edelman: Variable regions of heavy and light polypeptide chains of the same yG-immunoglobulin molecule. Proc. nat. Acad. Sci. (Wash.) 61, 168 (1968).

    Article  CAS  Google Scholar 

  • Gray, W. R., W. J. Dreyer, and L. Hood: Mechanism of antibody synthesis: size differences among x-chains. Science 155, 465 (1967).

    Article  PubMed  CAS  Google Scholar 

  • Green, I., P. Vassalli, and B. Benacerraf: Cellular localization of anti-DNP-PLL and anti-conveyor albumin antibodies in genetic nonresponder guinea pigs immunized with DNPPLL albumin complexes. J. exp. Med. 125, 527 (1967a).

    Article  PubMed  CAS  Google Scholar 

  • Green, I., P. Vassalli, and B. Benacerraf, V. Nussenzweig, and B. Benacerraf: Specificity of the antibodies produced by single cells following immunization with antigens bearing two types of antigenic determinants. J. exp. Med. 125,511 (1967 b).

    Google Scholar 

  • Haber, E.: Recovery of antigenic specificity after denaturation and complete reduction of disulfide bridges in a papain fragment of antibody. Proc. nat. Acad. Sci. (Wash.) 52, 1099 (1964).

    Article  CAS  Google Scholar 

  • Hilschenann, N.: The chemical structure of immunoglobulins. Proc. 11th Congr. int. Soc. Blood Transf., Sydney 1966, No. 29, Part 2, 501. Basel/New York: Karger 1968.

    Google Scholar 

  • Hilschenann, N.: Die chemische Struktur von zwei Bence-Jones-Proteinen (Roy and Cum.) vom x-Typ. Hoppe-Seylers Z. physiol. Chem. 348, 1077 (1967 a).

    Google Scholar 

  • Hilschenann, N.: Zum Mechanismus der Antikörperbildung. Hoppe-Seylers Z. physiol. Chem. 348, 1291 (1967 b).

    Google Scholar 

  • Hilschmann, N.: Die vollständige Aminosäuresequenz des Bence-Jones Proteins Cum (x-Typ). Hoppe-Seylers Z. physiol. Chem. 348, 1718 (1967 c).

    Google Scholar 

  • Hilschmann, N.:, and L. C. Craig: Amino acid sequence studies with Bence-Jones proteins. Proc. nat. Acad. Sci. (Wash.) 53, 1403 (1965).

    Google Scholar 

  • Hilschmann, N.: , H. U. Barnikol, M. Hess, B. Langer, H. Ponstingl, M.Steinmetz-Kayne, L. Suter, and S. Watanabe: Structural studies on immunoglobulins and their genetic implications for antibody formation. Proc. 5th FEBS-Meeting, Prague 1968. London: Academic Press Inc. (in press).

    Google Scholar 

  • Hood, L., W. R. Gray, B. G. Sanders, and W. J. Dreyer: Light chain evolution. Cold Spr. Harb. Symp. quant. Biol. 32, 133 (1967).

    CAS  Google Scholar 

  • Huisman, T. H. J., G. Brandt, and J. B. Wilson: The structure of goat hemoglobins. II. Structural studies of the a-chains of the hemoglobins A and B. J. biol. Chem. 243, 3675 (1968).

    PubMed  CAS  Google Scholar 

  • Jerne, N. K.: The natural-selection theory of antibody formation. Proc. nat. Acad Sci. (Wash.) 41, 849 (1955).

    Article  CAS  Google Scholar 

  • Kabat, E. A.: Kabat and Meyer’s Experimental Immunochemistry, 2nd. ed. Springfield (Ill.): Thomas 1961.

    Google Scholar 

  • Koshland, M. E., and F. M. Engelberger: Differences in the amino acid composition of two purified antibodies from the same rabbit. Proc. nat. Acad. Sci. (Wash.) 50, 61 (1963).

    Article  CAS  Google Scholar 

  • Kunkel, H. G.: Myeloma proteins and antibodies. Harvey Lect. 59, 219 (1965).

    CAS  Google Scholar 

  • Langer. B., M. Steinmetz-Kayne u. N. Hilschmann: Die vollständige Aminosäuresequenz des Bence-Jones Proteins New (.i-Typ). Subgruppen im variablen Teil bei Immunglobulin-L-Ketten vom.l-Typ. Hoppe-Seylers Z. physiol. Chem. 349, 945 (1968).

    Google Scholar 

  • Mannik, M.: Variability in the specific interactions of H- and L-chains of yG-globulins. Biochemistry 6, 134 (1967).

    Article  PubMed  CAS  Google Scholar 

  • Marchalonis, J. J., and G. M. Edelman: Antibodies in the primary immune response of the Sea Lamprey, Petromyzon Marinus. J. exp. Med. 127, 891 (1968).

    Article  PubMed  CAS  Google Scholar 

  • Martensson, L.: Genes and immunoglobulins. Vox Sang. (Basel) 11, 521 (1966).

    CAS  Google Scholar 

  • Milstein, C.: Interchain disulphide bridge in Bence-Jones proteins and in y-globulin B chains. Nature (Lond.) 205, 1172 (1965).

    Article  Google Scholar 

  • Milstein, C.: Variations in the amino-acid sequence near the disulphide bridges of immunoglobulin x-chains. Nature (Lond.) 209, 370 (1966a).

    Article  CAS  Google Scholar 

  • Milstein, C.: Chemical structure of light chains. Proc. roy. Soc. B 166 138 (1966 b).

    Google Scholar 

  • Milstein, C.: Immunoglobulin x-chains. Comparative sequences in selected streches of Bence-Jones proteins. Biochem. J. 101 352 (1966 c).

    Google Scholar 

  • Milstein, C.: , J. B. Clegg, and J. M. Jarvis: C-terminal half of immunoglobulin 2-chains. Nature (Lond.) 214, 270 (1967 a).

    Google Scholar 

  • Milstein, C.: Linked groups of residues in immunoglobulin x-chains. Nature (Lond.) 216 330 (1967 b).

    Google Scholar 

  • Milstein, C.: Studies on the variability of immunoglobulin sequence. Cold Spr. Harb. Symp. quant. Biol. 32, 31 (1967 c).

    Google Scholar 

  • Milstein, C.: Variations in the C-terminal half of immunoglobulin 2-chains. Biochem. J. 104 28 c (1967 d).

    Google Scholar 

  • Muller, H. J.: The gene material as the initiator and the organizing basis of life. Heritage from Mendel, R. A. Bring, and E. D. Styles, Eds., Madison, The University of Wisconsin Press, 1967.

    Google Scholar 

  • Natvig, J. B., H. G. Kunkel, and T. Gedde-Dahl Jr.: Genetic studies of the heavy chain subgroups of yG globulin. Recombination between the closely linked cistrons. Nobel Symp. 3, Gamma Globulins, J. Killander, Ed. Stockholm Almqvist and Wiksell 1967.

    Google Scholar 

  • Niall, H. D., and P. Edman: Two structurally distinct classes of x-chains in human immunoglobulins. Nature (Load.) 216, 262 (1967).

    Article  CAS  Google Scholar 

  • Pauling, L A theory of the structure and process of formation of antibodies. J. Amer. them. Soc. 62, 2643 (1940).

    Article  Google Scholar 

  • Pernis, B.: Relationships between the heterogeneity of immunoglobulins and the differentiation of plasma cells. Cold Spr. Harb. Symp. quant. Biol. 32, 333 (1967).

    CAS  Google Scholar 

  • Pernis, B.:, G. Chiappino, A. S. Kelus, and P. G. H. Gell: Cellular localization of immunoglobulins with different allotypic specificities in rabbit lymphoid tissues. J. exp. Med. 122, 853 (1965).

    Article  PubMed  CAS  Google Scholar 

  • Pollara, B., A. Suran, G. Finstad, and R. A. Good: N-terminal amino acid sequences of im- munoglobulin chains in polyodon spathula. Proc. nat. Acad. Sci. (Wash.) 59, 1307 (1968).

    Article  CAS  Google Scholar 

  • Ponstingl, H., M. Hess and N. Hilschmann: Die vollständige Aminosäuresequenz des BenceJones-Proteins Kern. Eine neue Untergruppe der Immunglobulin-L-Ketten vom A-Typ. Hoppe-Seylers Z. physiol. Chem. 349, 867 (1968).

    CAS  Google Scholar 

  • Ponstingl, H., M. Hess and N. Hilschmann, B. Langer, M. Steinmetz-Kayne and N. Hilschmann: Über einen Aminosäureaustausch im konstanten Teil eines Bence-Jones Proteins vom A-Typ. Hoppe-Seylers Z. physiol. Chem. 348, 1213 (1967).

    CAS  Google Scholar 

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

    PubMed  CAS  Google Scholar 

  • Press, E. M., and P. J. Piggot: The chemical structure of the heavy chain of human immunoglobulin G. Cold Spr. Harb. Symp. quant. Biol. 32, 45 (1967).

    CAS  Google Scholar 

  • Putnam, F. W., T. Shinoda, K. Titani, and M. Wilder Immunoglobulin structure: Variation in amino acid sequence and length of human lambda light chains. Science 157, 1050 (1967).

    Google Scholar 

  • Rudloff, V., M. Zellenik u. G. Braunitzer: Zur Phylogenie des Hämoglobinmoleküls. Untersuchungen am Hämoglobin des Flußneunauges (Lampetra fluviatilis). Hoppe-Seylers Z. physiol. Chem. 344, 284 (1966).

    CAS  Google Scholar 

  • Shapiro, A. L., M. D. Scharff, J. V. Maizel, and J. V. Uhr: Polyribosomal synthesis and as-

    Google Scholar 

  • sembly of the H and L chains of y-globulin. Proc. nat. Acad. Sci. (Wash.) 56, 216 (1966). Singer, S. J., and N. O. Thorpe: On the location and structure of the active sites of antibody molecules. Proc. nat. Acad. Sci. (Wash.) 60, 1371 (1968).

    Google Scholar 

  • Smithies, O.: Antibody variability. Science 157, 267 (1967).

    Article  PubMed  CAS  Google Scholar 

  • Suran, A. A., and B. W. Papermaster: N-terminal sequences of heavy and light chains of leopard shark immunoglobulins• Evolutionary implications. Proc. nat. Acad. Sci. (Wash.) 58, 1619 (1967).

    Article  CAS  Google Scholar 

  • Suter, L., H. U. Barnikol, S. Watanabe, and N. Hilschmann • Hoppe-Sylers Z. physiol. Chem. 350, 275 (1969).

    Google Scholar 

  • Schroeder, W. A., T. H. J. Huisman, J. R. Shelton, J. B. Shelton, E. F. Kleihauer, A. M. Dozy, and B. Robberson: Evidence for multiple structural genes for the y-chain of human fetal hemoglobin. Proc. nat. Acad. Sci. (Wash.) 60, 537 (1968).

    Article  CAS  Google Scholar 

  • Steinberg, A. G.: Progress in the study of genetically determined human gamma globulin types (the Gm and Inv groups). Progress in medical genetics, Vol. II. New York-London: Grune and Stratton 1962.

    Google Scholar 

  • Titani, K., E. Whitley, and F. W. Putnam• Immunoglobulin structure: Variation in the sequence of Bence-Jones proteins. Science 152, 1513 (1966).

    Google Scholar 

  • Valentine, R. C., and N. M. Greene: Electron microscopy of an antibody-hapten complex. J. molec. Biol. 27, 615 (1967).

    Article  PubMed  CAS  Google Scholar 

  • Waldenström, J.: Studies on conditions associated with disturbed gamma globulin formation (gammopathies). Harvey Lect. 56, 211 (1961).

    Google Scholar 

  • Whitehouse, H. L. K.: Crossover model of antibody variability. Nature (Loud.) 215, 371 (1967).

    Article  CAS  Google Scholar 

  • Whitney, Ch. L., and Ch. Tanford: Recovery of specific activity after complete unfolding and reduction of an antibody fragment. Proc. nat. Acad. Sci. (Wash.) 53, 524 (1965).

    Article  CAS  Google Scholar 

  • Williamson, A. R., and B. A. Askonas: Biosynthesis of immunoglobulins The separate classes of polyribosomes synthesizing heavy and light chains. J. molec. Biol. 23, 201 (1967).

    Article  PubMed  CAS  Google Scholar 

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Author information

Authors and Affiliations

  1. Max-Planck-Institut für experimentelle Medizin, Abteilung Chemie, Arbeitsgruppe Immunochemie, 34 Göttingen, Hermann-Rein-Straße 3, Germany

    Dr. N. Hilschmann

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  1. Dr. N. Hilschmann
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  2. H. U. Barnikol
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  3. M. Hess
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  4. B. Langer
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  5. H. Ponstingl
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  6. M. Steinmetz-Kayne
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  7. L. Suter
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  8. S. Watanabe
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Editor information

Editors and Affiliations

  1. Max-Planck-Instituts für Immunbiologie, Stübeweg 51, 7800, Freiburg-Zähringen, Deutschland

    Otto Westphal (Direktor) (Direktor)

  2. Medizinischen Klinik der Universität, Olfried-Müller-Straße, 7400, Tübingen, Deutschland

    Hans-Erhard Bock (Direktor) (Direktor)

  3. Instituts für experimentelle Pathologie, Farbenfabriken Bayer AG, 5600, Wuppertal-Elberfeld, Deutschland

    Ekkehard Grundmann (Vorstand) (Vorstand)

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Hilschmann, N. et al. (1969). Structure and Formation of Antibodies. In: Westphal, O., Bock, HE., Grundmann, E. (eds) Current Problems in Immunology. Bayer-Symposium, vol 1. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-29237-2_8

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  • DOI: https://doi.org/10.1007/978-3-662-29237-2_8

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  • Print ISBN: 978-3-662-27746-1

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