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The Structure of Antibodies

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Biochemistry of Antibodies
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Abstract

Considerable difficulties are involved in the study of immunoglobulins. Data on N-terminal amino acids, which have been useful for an understanding of the structure of many proteins, have not been of any essential help here. As mentioned earlier (cf. Chapter III), only one N-terminal amino acid — alanine (one mole alanine per mole protein) —plus a small quantity of aspartic acid and serine, has been found in rabbit γG-globulins. Three to five N-terminal amino acids have been found in equine and bovine γ-globulins, but their sum was less than one mole per mole protein. The γ-globulins of pigs and man contain two principal N-terminal amino acids. After reduction or denaturation, no new N-terminal amino acid residues appear. Hence, a reliable evaluation of the number of peptide chains in the immunoglobulin molecule cannot be obtained from these investigations.

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Literature Cited

  1. A. E. Gurvich, L. M. Gubernieva, and K. N. Myasoedova, “Comparison of enzymic hydrolyzates of nonspecific γ -globulins and antibodies,” Biokhimiya 26(3):468 (1961).

    CAS  Google Scholar 

  2. A. E. Gurvich and R. S. Nezlin, “Nomenclature for human immunoglobulins,” Biokhimiya 30(2):443 (1965).

    Google Scholar 

  3. L. N. Kaigorodova, E. D. Kaversneva, “Chemical characterization of a cryogel-macroglobulin,” Molec. Biology (USSR) 1(2):224 (1967).

    CAS  Google Scholar 

  4. A.Ya. Kul’berg and I. A. Tarkhanova, “On the problem of papain cleavage of immune y-globulin,” Vopr. Med. Khim. 7(5):520 (1961).

    PubMed  Google Scholar 

  5. A. Ya. Kul’berg and I. A. Tarkhanova, “Role of disulfide bonds in the structure of the antibody binding site,” Biokhimiya 29(2):246 (1964).

    Google Scholar 

  6. N. E. Kuchinskaya, A. Ya. Kul’berg, and V. S. Tsvetkov, “Immunochemical analysis of papain-cleavage products of bovine γ -globulin,” Biokhimiya 30(5):1065 (1965).

    CAS  Google Scholar 

  7. R. S. Nezlin, “Peptide chains of γ -globulins and antibodies,” Usp. Sovrem. Biol. 58(2):201 (1964).

    PubMed  CAS  Google Scholar 

  8. R. S. Nezlin and L. M. Kulpina, “Cellulose-fixed immunoglobulin subunits,” Immunochemistry 4(4):296 (1967).

    Google Scholar 

  9. V.I. Okulov, “Effect of cleavage of disulfide bonds on various properties of bovine γ -globulin,” in: Proteins in Medicine and National Economy [in Russian], Naukova Dumka, Kiev (1965), p. 53.

    Google Scholar 

  10. D. V. Stefani and A. Ya. Kul’berg, “Immunological analysis of products of papain proteolysis of horse antidiphtheria antitoxic γ -globulin,” Vopr. Med. Khim. 10(3):279 (1964).

    PubMed  CAS  Google Scholar 

  11. D. V. Stefani, A. Ya. Kul’berg, and K. L. Shakhanina, “Distinguishing features of the immunochemical structure of horse antitoxic ß2A-globulin,” Vopr. Med. Khim. 11(4):34 (1965).

    PubMed  CAS  Google Scholar 

  12. I. A. Tarkhanova and A. Ya. Kul’berg, “Participation of tryptophan in the structure of the antibody binding site,” Vopr. Med. Khim. 8(2): 163 (1962).

    PubMed  Google Scholar 

  13. F. Franek and R. S. Nezlin, “Study of the role of different peptide chains of antibodies in the antigen — antibody reaction,” Biokhimiya 28(2): 193 (1963).

    CAS  Google Scholar 

  14. R. Arnon, M. Sela, A. Yaron, and H. A. Sober, “Polylysine-specific antibodies and their reaction with oligolysines,” Biochemistry 4(5):948 (1965).

    PubMed  CAS  Google Scholar 

  15. R. E. Balliex, G. M. Bernier, K. Tominage, and F. W. Putnam, “Gamma globulin antigenic types defined by heavy determinants, ” Science 145(3628):167 (1964).

    Google Scholar 

  16. B. Benacerraf, C. Merryman, and R. A. Binaghi, “Studies of the chains of guinea pig and rat anti-2,4-dinitrophenyl antibodies,” J. Immunol. 93(4):618 (1964).

    PubMed  CAS  Google Scholar 

  17. C. C. F. Blake, D. F. Koenig, E. A. Mair, A. C. T. North, D. C. Phillips, V. R. Sarma, “Structure of hen egg-white lysozyme, ” Nature 206(4986):757 (1965).

    PubMed  CAS  Google Scholar 

  18. W. B. Bridgman, “The peptic digestion of human gamma globulin,” J. Am. Chem. Soc. 68(5):857 (1946).

    PubMed  CAS  Google Scholar 

  19. C. E. Buckley, P. L. Whitney, and C. Tanford, “The unfolding and renaturation of a specific univalent antibody fragment,” Proc. Nat. Acad. Sci. USA 50(5): 827(1963).

    PubMed  CAS  Google Scholar 

  20. M. Burrand and D. E. Koshland, “Use of “reporter groups” in structure function studies of proteins,” Proc. Nat. Acad. Sci. USA 52(4):1017 (1964).

    Google Scholar 

  21. H. J. Cahnmann, R. Arnon, M. Sela, “Isolation and characterization of active fragments obtained by cleavage of immunoglobulin G with cyanogen bromide,” J. Biol. Chem. 241(14):3247 (1966).

    PubMed  CAS  Google Scholar 

  22. A. O. Carbonara and J. F. Heremans, “Subunits of normal and pathological 1A-globulins (ß2A-globulins),” Arch. Biochem. Biophys. 102(1):137 (1963).

    PubMed  CAS  Google Scholar 

  23. R. E. Cathou and E. Haber, “Structure of the antibody combining site. I. Hapten stabilization of antibody conformation,” Biochemistry 6(2):513 (1967).

    PubMed  CAS  Google Scholar 

  24. J.J. Cebra, “The effect of sodium dodecylsulfate on intact and insoluble papain hydrolyzed immune globulin,” J. Immunol. 92(6):977 (1964).

    PubMed  CAS  Google Scholar 

  25. J.J. Cebra, “Studies on the combining sites of the protein antigen silk fibroin. III. Inhibition of the silk fibroin — antifibroin system by peptides derived from the antigen,” J. Immunol. 86(2):205 (1961).

    PubMed  CAS  Google Scholar 

  26. J. J. Cebra, “Some properties of reductively fragmented gamma-2 and gamma-1 M immune globulins,” in: Molecular and Cellular Basis of Antibody Formation, Academic Press, New York (1965), p. 103.

    Google Scholar 

  27. J. J. Cebra, D. Givol, and E. Katchalski, “Soluble complexes of antigen and antibody complexes,” J. Biol. Chem. 237(3):751 (1962).

    PubMed  CAS  Google Scholar 

  28. J. J. Cebra, D. Givol, H. I. Silman, and E. Katchalski, “A two-stage cleavage of rabbit globulin by a water-insoluble papain preparation followed by cysteine,” J. Biol. Chem. 236(6):1720 (1961).

    PubMed  CAS  Google Scholar 

  29. H. Chaplin, S. Cohen, and E. M. Press, “Preparations and properties of the peptide chains of normal human 19 S-globulin (IgM),” Biochem. J. 95(1):256 (1965).

    PubMed  CAS  Google Scholar 

  30. T. J. Coleman, R. D. Marshall, and M. Potter, “ Preparation of a glycopeptide from an immunoglobulin K polypeptide chain from the mouse. ” Biochim. Biophys Acta. 147(2):396 (1967).

    PubMed  CAS  Google Scholar 

  31. S. Cohen, “Properties of the separated chains of human gamma-globulin,” Nature 197(4864):253 (1963).

    PubMed  CAS  Google Scholar 

  32. S. Cohen, “Properties of the peptide chains of normal and pathological human-globulins,” Biochem. J. 89(2):334 (1963).

    PubMed  CAS  Google Scholar 

  33. S. Cohen and S. Gerden, “Dissociation of n- and A.- chains from reduced human immunoglobulins,” Biochem. J. 97(2):460 (1965).

    PubMed  CAS  Google Scholar 

  34. S. Cohen and C. Milstein, “Structure of antibody molecules,” Nature 214(5087): 449 (1967).

    PubMed  CAS  Google Scholar 

  35. S. Cohen and R. R. Porter, “Heterogeneity of the peptide chains of y -globulin,” Biochem. J. 90(2):278 (1964).

    PubMed  CAS  Google Scholar 

  36. S. Cohen and R. R. Porter, “Structure and biological activity of immunoglobulins,” Advan. Immunol. 4:287 (1964).

    CAS  Google Scholar 

  37. F. E. Cominga, “A third γ-globulin chain?,” Lancet 2(7311):786 (1963).

    Google Scholar 

  38. R. S. Criddle, “Dissociation and separation of gamma globulin into subunits,” Arch. Biochem. Biophys. 106(1–3):101 (1964).

    PubMed  CAS  Google Scholar 

  39. J. Crumpton and J. M. Wilkinson, “Amino acid compositions of human and rabbit γ-globulins and the fragments produced by reduction,” Biochem. J. 88(2):228 (1963).

    PubMed  CAS  Google Scholar 

  40. D. R. Davies, “A correlation between amino acid composition and protein structure,” J. Mol. Biol. 9(2):605 (1964).

    PubMed  CAS  Google Scholar 

  41. H. F. Deutsch, E. R. Stiehm, and J.J. Mortone, “Action of papain on human serum globulins,” J. Biol. Chem. 236(8):2216 (1961).

    PubMed  CAS  Google Scholar 

  42. K. Y. Dorrington, M. H. Larlengo, and C. Tanford, “Conformational change and complementarity in the combination of H and L chains of immunoglobulin G. Proc. Nat. Acad. Sci. USA, 58(3996) (1967).

    Google Scholar 

  43. G. M. Edelman, “Dissociation of γ-globulins,” J. Am. Chem. Soc. 81(12):3155 (1959).

    CAS  Google Scholar 

  44. G. M. Edelman and B. Benacerraf, “On structural and functional relations between antibodies and proteins of the gamma-system,” Proc. Nat. Acad. Sci. USA 48(6):1035 (1962).

    PubMed  CAS  Google Scholar 

  45. G. M. Edelman, B. Benacerraf, Z. Ovary, and M. D. Poulik, “Structural differences among antibodies of different specificities,” Proc. Nat. Acad. Sci. USA 47(11):1751 (1961).

    PubMed  CAS  Google Scholar 

  46. C. A. Edelman and J. A. Gaily, “The nature of Bence—Jones proteins. Chemical similarities of polypeptide chains of myeloma globulins and normal γ -globulins,” J. Exp. Med. 116(2):2207 (1962).

    Google Scholar 

  47. G. M. Edelman, “Formation of active 7 S antibody molecules by reassociation of polypeptide chains,” in: Molecular and Cellular Basis of Antibody Formation, Academic Press, New York (1965), p. 113.

    Google Scholar 

  48. G. M. Edelman, J. F. Heremans, M. Heremans, and H. G. Kunkel, “Immunological studies of human globulin. Relation of precipitin line of whole globulin to those of the fragments produced by papain,” J. Exp. Med. 112(1):203 (1960).

    PubMed  CAS  Google Scholar 

  49. G. M. Edelman and J. A. Gaily, “A model for the 7 S antibody molecule,” Proc. Nat. Acad. Sci. USA 51(5):846 (1964).

    PubMed  CAS  Google Scholar 

  50. G. M. Edelman and E.A. Kabat “Studies on human antibodies. I. Starch gel electrophoresis of the dissociated polypeptide chains,” J. Exp. Med. 119(3):443 (1963).

    Google Scholar 

  51. G. M. Edelman, D. E. Olins, J. A. Gaily, and N. D. Zinder, “Reconstitution of immunologic activity by interaction of polypeptide chains of antibodies,” Proc. Nat. Acad. Sci. USA 50(4):753 (1963).

    PubMed  CAS  Google Scholar 

  52. G. M. Edelman and M. D. Poulik, “Studies on structural units of the gamma globulins,” J. Exp. Med. 113(5):861 (1961).

    PubMed  CAS  Google Scholar 

  53. H. N. Eisen, J. R. Little, K. Osterland, and E. S. Simms, “A myeloma G-protein with antibody (anti-2, 4-dinitrophenyl) activity.” Abstr. Cold Springs Harbor Symp., p. 13 (1967).

    Google Scholar 

  54. H. N. Eisen and J. H. Pearce, “The nature of antibodies and antigens,” Ann. Rev. Microbiol. 16:101(1962).

    CAS  Google Scholar 

  55. C. J. Epstein, R. F. Goldberger, and C. B. Anfinsen, “The genetic control of tertiary protein structure: studies with model system,” Cold Spring Harbor Symp. Quart. Biol. 28:439 (1964).

    Google Scholar 

  56. J. L. Fahey, “Heterogeneity of γ-globulins,” Advan. Immunol. 2(41) (1962).

    Google Scholar 

  57. J. L. Fahey and B. A. Askonas, “Enzymatically produced subunits of proteins formed by plasma cells in mice. I. γ-globulin and myeloma proteins,” J. Exp. Med. 115(3):623 (1962).

    PubMed  CAS  Google Scholar 

  58. J. W. Fenton and S.J. Singer, “Affinity labeling of antibodies to the p-azo-phenyltrimethylammonium hapten and a structural relationship among antibody active sites of different specificities,” Biochem. Biophys. Res. Commun. 20(3):315 (1965).

    PubMed  CAS  Google Scholar 

  59. J. B. Fleischman, “The synthesis of γ -globulin by rabbit lymph node cells,” J. Immunol. 91(2):163 (1963).

    PubMed  CAS  Google Scholar 

  60. J. B. Fleischman, R. R. Porter, and R. H. Pain, “Reduction of γ-globulins,” Arch. Biochem. Biophys., Suppl. 1, p. 174 (1962).

    CAS  Google Scholar 

  61. J. B. Fleischman, R.R. Porter, and E. M. Press, “The arrangement of the peptide chains in γ-globulin,” Biochem. J. 88(2):220 (1963).

    PubMed  CAS  Google Scholar 

  62. M. Fougereau and G. M. Edelman, “Resemblance of the gross arrangement of polypeptide chains in reconstituted and native γ -globulins,” Biochemistry 3(8):1120 (1964).

    PubMed  CAS  Google Scholar 

  63. M. Fougereau and G. M. Edelman, “Corroboration of recent models of the γ G-immunoglobulin molecule,” J. Exp. Med. 121(3):373 (1965).

    PubMed  CAS  Google Scholar 

  64. M. Fougereau, D. E. Olins, and G. M. Edelman, “Reconstitution of antiphage antibodies from L and H polypeptide chains and the formation of interspecies molecular hybrids,” J. Biol. Chem. 120(3):349 (1964).

    CAS  Google Scholar 

  65. F. Franek, “Dissociation of animal 7 S γ-globulins by cleavage of disulfide bonds,” Biochem. Biophys. Res. Commun. 4(1):28 (1961).

    PubMed  CAS  Google Scholar 

  66. F. Franek, “Some properties of higher subunits of pig γ G-globulin,” Collection Czech. Chem. Commun. 30(6):1947 (1965).

    CAS  Google Scholar 

  67. F. Franek, and B. Keil, “Structural differences between γ-globulin chains,” Collection Czech. Chem. Commun. 29(3):847 (1964).

    CAS  Google Scholar 

  68. F. Franek, O. Kotynek, L. Simek, and J. Zikan, “S-Sulfonated antidinitrophenyl antibodies. Some specific features of the interaction between isolated H and L subunits,” in: Molecular and Cellular Basis of Antibody Formation, Academic Press, New York (1965), p. 125.

    Google Scholar 

  69. F. Franek and R.S. Nezlin, “Recovery of antibody combining activity by interaction of different peptide chains isolated from purified horse antitoxins,” Folia Microbiol. 8(2):128 (1963).

    CAS  Google Scholar 

  70. F. Franek, R. S. Nezlin, and F. Skvaril, “Antibody binding capacity of different peptide chains isolated from digested and purified horse diphtheria antitoxin,” Folia Microbiol. 8(4):197 (1963).

    CAS  Google Scholar 

  71. F. Franek, V. Paces, B. Keil, and F. Sorn, “On proteins. CXI. Isolation of electrophoretically homogeneous components of normal pig γ G-globulin light chains and demonstration of their structural heterogeneity,” Collection Czech. Chem. Commun. 32(9):3242 (1967).

    CAS  Google Scholar 

  72. F. Franek and I. Riha, “Purification and structural characterization of 5 S γ -globulin in newborn pigs,” Immunochemistry 1(1):49 (1964).

    PubMed  CAS  Google Scholar 

  73. F. Franek and J. Zikan, “Limited cleavage of disulfide bonds of pig γ -globulin by S-sulfonation,” Collection Czech. Chem. Commun. 29(6): 1401 (1964).

    CAS  Google Scholar 

  74. F. Franek and O. M. Zorina, “On proteins. CX. Isolation and characterization of lambda and pi chains representing structural types of pig γ G-globulin light chains,” Collection Czech. Chem. Commun. 32(9):3229 (1967).

    CAS  Google Scholar 

  75. B. Frangione and E. C. Franklin, “Structural studies of human immunoglobulins. Differences in the Fd fragments of the heavy chains of G myeloma proteins,” J. Exp. Med. 122(1): 1 (1965).

    PubMed  CAS  Google Scholar 

  76. B. Frangione, F. Prelli, and E. C. Franklin, “The structure of Fd fragments of myeloma proteins,” Immunochemistry 4(2):95 (1967).

    CAS  Google Scholar 

  77. B. Frangione and E. C. Franklin, “Structural studies of human immunoglobulins. Differences in primary structure of heavy chains of normal and pathologic G, A, and Mimmunoglobulins,” Arch. Biochem. Biophys. 111(3):603 (1965).

    PubMed  CAS  Google Scholar 

  78. E. C. Franklin, “Structural units of human 7 S γ -globulin,” J. Clin. Invest. 39(12):1933 (1960).

    PubMed  CAS  Google Scholar 

  79. E. C. Franklin, “Structural studies of human 7 S γ-globulin (G immunoglobulin). Further observations of a naturally occurring protein related to the crystallizable (fast) fragment,” J. Exp. Med. 120(5):691 (1964).

    PubMed  CAS  Google Scholar 

  80. E. C. Franklin and B. Frangione, “Two serologically distinguishable subclasses of mu-chains of human macroglobulins,” J. Immunol. 99(4):810 (1967).

    PubMed  CAS  Google Scholar 

  81. E. C. Franklin, H. Fudenberg, B. Frangione, and M. Meltzer, “Structural basis for differences between γ -globulins of different genetic (Gm) types. Studies of normal γ-globulins and para-proteins,” in: Molecular and Cellular Basis of Antibody Formation, Academic Press, New York (1965), p. 193.

    Google Scholar 

  82. E. C. Franklin, J. Lowenstein, B. Bigelow, and M. Meltzer, “Heavy chain disease — a new disorder of serum γ -globulins. Report of the first case,” Am. J. Med. 37(3):327 (1964).

    Google Scholar 

  83. S. Fuchs and M. Sela, “Preparation and characterization of poly-DL-alanyl rabbit γ -globulin,” J. Biol. Chem. 240(3):327 (1964).

    Google Scholar 

  84. M. H. Freedman and M. Sela, “Recovery of antigenic activity upon reoxidation of completely reduced polyalanyl rabbit immunoglobulin Gm,” J. Biol. Chem. 241(10):2383 (1966).

    PubMed  CAS  Google Scholar 

  85. M. H. Freedman and M. Sela, “Recovery of specific activity upon reoxidation of completely reduced polyalanyl rabbit antibody,” J. Biol. Chem. 241(22):5225 (1966).

    PubMed  CAS  Google Scholar 

  86. H.H. Fudenberg, G. Drews, and A. Nisonoff, “Serological demonstration of dual specificity of rabbit bivalent hybrid antibody,” J. Exp. Med. 119(1):151 (1964).

    PubMed  CAS  Google Scholar 

  87. J. A. Gaily and G. M. Edelman, “Protein-protein interactions among L-polypeptide chains of Bence-Jones proteins and human γ-globulins,” J. Exp. Med. 119 (5): 817(1964).

    Google Scholar 

  88. L. Gyenes, A. H. Sehon, S.O. Freedman, and Z. Ovary, “The properties of fragments of skin-sensitizing and blocking antibodies as revealed by the Prausnitz —Küstner, passive cutaneous anaphylaxis and hemagglutination reactions,” Intern. Arch. Allergy and Appl. Immunol. 24:106 (1964).

    CAS  Google Scholar 

  89. D. Gitlin and E. Merler, “A comparison of the peptides released from related rabbit antibodies by enzymatic hydrolysis,” J. Exp. Med. 114(2):317 (1961).

    Google Scholar 

  90. D. Givol, “The cleavage of rabbit immunoglobulin G by trypsin after mild reduction and aminoethylation,” Biochem. J. 104(3):390 (1967).

    Google Scholar 

  91. D. Givol and R. R. Porter, “The chemical structure of the heavy chain of rabbit immunoglobulin G (IgG),” Israel J. Chem. 4:68 (1966).

    Google Scholar 

  92. D. Givol and M. Sela, “A comparison of fragments of rabbit antibodies and normal γ-globulin by the peptide-map technique,” Biochemistry 3(3):451 (1964).

    PubMed  CAS  Google Scholar 

  93. E. F. Gold, D. L. Knight, and F. Haurowitz, “Peptide maps of antibodies against an antigen containing two different determinant groups,” Biochem. Biophys. Fes. Commun. 18(1):76 (1965).

    CAS  Google Scholar 

  94. J. W. Goodman, “Antigenic determinants in fragments of gamma globulin from rabbit serum,” Science 139(3561):1292 (1963).

    PubMed  CAS  Google Scholar 

  95. J. W. Goodman, “Immunologically active fragments of rabbit y -globulin,” Biochemistry 3(6):857 (1964).

    PubMed  CAS  Google Scholar 

  96. J. W. Goodman, “Heterogeneity of rabbit γ -globulin with respect to cleavage by papain,” Biochemistry 4(11):2350 (1965).

    CAS  Google Scholar 

  97. J. W. Goodman and E. A. Kabat, “Immunochemical studies on cross = reactions of anti-pneumococcal sera,” J. Immunol. 84(4):333 (1960).

    PubMed  CAS  Google Scholar 

  98. D. Griffin, D. K. Tachibana, B. Nelson, and L. T. Rosenberg, “Contribution of tryptophan to the biological properties of antidinitrophenyl antibody,” Immunochemistry 4(1):23 (1967).

    PubMed  CAS  Google Scholar 

  99. J. L. Groff and F. Haurowitz, “Comparison of the peptide maps of antibodies against an acidic and a basic determinant group, ” Immunochemistry 1(1):31 (1964).

    PubMed  CAS  Google Scholar 

  100. W. R. Gray, W.J. Dreyer, and L. Hood, “Mechanism of antibody synthesis: size differences between mouse kappa chains,” Science 155(3761):465 (1967).

    PubMed  CAS  Google Scholar 

  101. A. L. Grossberg, C. C. Chen, L. Rendina, and D. Pressman, “Specific cation effects with antibody to a hapten with a positive charge, ” J. Immunol. 88(5):600 (1962).

    PubMed  CAS  Google Scholar 

  102. A. L. Grossberg and D. Pressman, “Effect of acetylation on active site of several antihapten antibodies: further evidence for the presence of tyrosine in each site,” Biochemistry 2(1):90 (1963).

    PubMed  CAS  Google Scholar 

  103. A. L. Grossberg and O.A. Roholt, “Further evidence that antibody fragments in fractions I and II are from different kinds of antibody molecules,” Federation Proc. 21(2):28 (1962).

    Google Scholar 

  104. A. L. Grossberg, O. A. Roholt, and D. Pressman, “Different distribution of antibodies of two specificities among γ-globulins of an individual rabbit,” Biochemistry 2(5):989 (1963).

    PubMed  CAS  Google Scholar 

  105. A. L. Grossberg, P. Stelos, and D. Pressman, “Structure of fragments of antibody molecules as revealed by reduction of exposed disulfide bonds,” Proc. Nat. Acad. Sci. USA 48(7):1203 (1962).

    PubMed  CAS  Google Scholar 

  106. A. F. S. A. Habeeb, H. G. Cassidy, P. Stelos, and S. J. Singer, “Some studies of the chemical modification of antibodies, ” Biochem. Biophys. Acta 34(2):439 (1959).

    PubMed  CAS  Google Scholar 

  107. E. Haber, “Recovery of antigenic specificity after denaturation and complete reduction of disulfides in a papain fragment of antibody,” Proc. Nat. Acad. Sci. USA 52(4):1099 (1964).

    PubMed  CAS  Google Scholar 

  108. E. Haber and F.F. Richards, “The specificity of antigenic recognition of antibody heavy chain,” Proc. Roy. Soc, Ser. B 166(1003):176 (1966).

    CAS  Google Scholar 

  109. R. Heimer, E. R. Schwartz, R. L. Engle, and K. R. Woods, “The relationship of structure to the thermal solubility characteristics of a Bence—Jones protein,” Biochemistry 2(6):1380 (1963).

    PubMed  CAS  Google Scholar 

  110. R. L. Hill, R. Delaney, H. E. Lebovitz, and R. E. Fellows, “Studies on the amino acid sequence of heavy chains from rabbit immunoglobulin,” Proc. Roy. Soc, Ser. B 166(1003):159(1966).

    CAS  Google Scholar 

  111. N. Hilschmann and L. C. Craig, “Amino acid sequence studies with Bence-Jones proteins,” Proc. Nat. Acad. Sci. USA 53(6):1403 (1965).

    PubMed  CAS  Google Scholar 

  112. N. Hilschmann, “The chemical structure of two Bence—Jones proteins (Roy and Cum) of the K-type,” Hoppe-Seyler Z. Phys. Chem. 348(8):1077 (1967).

    CAS  Google Scholar 

  113. R. Hong, J. L. Palmer, and A. Nisonoff, “Univalence of half-molecules of rabbit antibodies,” J. Immunol. 94(4):603 (1965).

    PubMed  CAS  Google Scholar 

  114. R. Hong and A. Nisonoff, “Relative labilities of the two types of interchain disulfied bond of rabbit γ G- immunoglobulin,” J. Biol. Chem. 240(10):3883 (1965).

    PubMed  CAS  Google Scholar 

  115. Hsiao Shuhsi and F. W. Putnam, “The cleavage of human γ-globulin by papain,” J. Biol. Chem. 236(1):122 (1961).

    Google Scholar 

  116. V.M. Ingram, Hemoglobin and Its Abnormalities, Charles C. Thomas, Springfield, 111. (1961).

    Google Scholar 

  117. F. P. Inman and A. Nisonoff, “Reversible dissociation of fragment Fc of rabbit γ G-immunoglobulin,” J. Biol. Chem. 241(2):322 (1966).

    PubMed  CAS  Google Scholar 

  118. H. Jacot-Guillarmond and H. Isliker, “Reversible cleavage of subunits,” Vox Sanguinis 9(1):31 (1964).

    Google Scholar 

  119. H. Jaquet, B. Bloom, and J. J. Cebra, “Retention of antibody activity by re-ductively dissociated immune globulin,” Federation Proc. 22(2):496 (1963).

    Google Scholar 

  120. H. Jaquet, B. Bloom, and J.J. Cebra, “The reductive dissociation of rabbit immune globulin in sodium dodecylsulfate,” J. Immunol. 92(6):991 (1964).

    PubMed  CAS  Google Scholar 

  121. H. Jaquet and J. J. Cebra, “Comparison of two precipitating derivatives of rabbit antibody: fragment L dimer and the product of pepsin digestion,” Biochemistry 4(5):954 (1965).

    PubMed  CAS  Google Scholar 

  122. K. James and D. R. Stanworth, “Structural changes occurring in 7 S globulins,” Nature 202(4932):563 (1964).

    PubMed  CAS  Google Scholar 

  123. B. Jirgensons, D. Yonezawa, and V. Gorguraki, “Structural studies on human serum gamma-globulins and myeloma proteins. I. Fragmentation and denaturation of the globulins with detergent and alkali,” Makromol. Chem. 60:25 (1963).

    CAS  Google Scholar 

  124. B. Jirgensons, M. E. Adams-Mayne, V. Gorguraki, and P. J. Migliore, “Structure studies on human serum γ -globulins and reconstitution of the macro-molecules,” Arch. Biochem. Biophys. 111(2):283 (1965).

    PubMed  CAS  Google Scholar 

  125. D. Yonezawa, P. J. Migliore, S. C. Capetillo, and B. Jirgensons, “Structural studies on human serum gamma-globulins and myeloma proteins. II. Cleavage of disulfide bonds of globulins with sulfite and recombination of the fragments,” Makromol. Chem. 77:191 (1964).

    CAS  Google Scholar 

  126. E. A. Kabat, “Some configurational requirements and dimensions of the combining site on an antibody to a naturally occurring antigen,” J. Am. Chem. Soc. 76(14):3709 (1954).

    CAS  Google Scholar 

  127. E. A. Kabat, “Heterogeneity in extent of the combining regions of human antidextran,” J. Immunol. 77(6):377 (1956).

    PubMed  CAS  Google Scholar 

  128. E. A. Kabat, “The upper limit for the size of the human antidextran combining site,” J. Immunol. 84(1):82 (1960).

    PubMed  CAS  Google Scholar 

  129. E. A. Kabat, Experimental Immunochemistry, Charles C. Thomas, Springfield, 111. (1961).

    Google Scholar 

  130. E. A. Kabat, “The paucity of species-specific amino acid residues in the variable regions of human and mouse Bence—Jones proteins and its evolutionary and genetic implications,” Proc. Nat. Acad. Sci. USA 57(5): 1345 (1967).

    PubMed  CAS  Google Scholar 

  131. F. Karush, “The interaction of purified antibody with optically isomeric haptens,” J. Am. Chem. Soc. 78(21):5519.(1956).

    CAS  Google Scholar 

  132. F. Karush, “The interaction of purified anti-ß -lactoside antibody with haptens,” J. Am. Chem. Soc. 79(13):3380 (1957).

    CAS  Google Scholar 

  133. F. Karush, “Properties of papain-digested purified anti-hapten antibody,” Federation Proc. 18(1):1577 (1959).

    Google Scholar 

  134. F. Karush, “Immunologic specificity and molecular structure,” Advan. Immunol. 2:1 (1962).

    CAS  Google Scholar 

  135. M. E. Koshland, F. M. Engelberger, and S. M. Gaddone, “The effect of iodina-tion on the binding of haptene to arsonic acid,” J. Immunol. 89(4):517 (1962).

    PubMed  CAS  Google Scholar 

  136. M. E. Koshland, F. M. Engelberger, and S. M. Gaddone, “Identification of tyrosine at the active site of anti-p-azobenzenearsonic acid antibody,” J. Biol. Chem. 238(4):1349 (1963).

    PubMed  CAS  Google Scholar 

  137. M. E. Koshland, F. M. Engelberger, and S. M. Gaddone, “Evidence against the universality of a tyrosyl residue at antibody combining sites,” Immunochemistry 2:115 (1965).

    PubMed  CAS  Google Scholar 

  138. M. E. Koshland, F. Engelberger, and D.E. Koshland, “A general method for labeling of the active site of antibodies and enzymes,” Proc. Nat. Acad. Sci. USA 45(10): 1470 (1959).

    PubMed  CAS  Google Scholar 

  139. O. Kotynek and F. Franek, “Unequal importance of different polypeptide chains for the determination of antibody specificity in bovine antidinitro-phenyl antibodies,” Collection Czech. Chem. Commun. 30(9):3153 (1965).

    CAS  Google Scholar 

  140. V. P. Kreiter and D. Pressman, “Antibodies to a hapten with two determinant groups,” Immunochemistry 1(3):151 (1964).

    PubMed  CAS  Google Scholar 

  141. H. G. Kunkel and R. A. Prendergast, “Supergroups of γ A-immune globulins,” Proc. Soc. Exp. Biol. Med. 122(3):910 (1966).

    PubMed  CAS  Google Scholar 

  142. H. G. Kunkel, J. C. Allen, H. M. Grey, L. Martensson, and R. Grubb, “A relationship between H chain groups of 7 S γ-globulin and the Gm system,” Nature 203(4943):413 (1964).

    PubMed  CAS  Google Scholar 

  143. M. E. Lamm and P. A. Small, “Polypeptide chain structure of rabbit immunoglobulins. II. γ M-immunoglobulin,” Biochemistry 5(1):267 (1966).

    PubMed  CAS  Google Scholar 

  144. M. Lahav, R. Arnon, and M. Sela, “Biological activity of the cleavage product of human immunoglobulin G with cyanogen bromide,” J. Exp. Med. 125 (5):787(1967).

    PubMed  CAS  Google Scholar 

  145. K. Landsteiner, The Specificity of Serological Reactions, 2nd Edition, Harvard University Press, Cambridge (1945).

    Google Scholar 

  146. E. S. Lennox and M. Cohn, “Immunoglobulins,” Ann. Rev. Biochem. 36, Pt. 1:365 (1967).

    Google Scholar 

  147. B. B. Levine, “Studies on the dimensions of rabbit antibenzylpenicilloyl antibody combining sites,” J. Exp. Med. 117(1):161 (1963).

    PubMed  CAS  Google Scholar 

  148. J. R. Little and H. N. Eisen, “Evidence for tryptophan in the active sites of antibodies to polynitrobenzenes,” Biochemistry 6(10):3119 (1967).

    PubMed  CAS  Google Scholar 

  149. M. L. MacFadden and E. L. Smith, “Free amino acid groups and N-terminal sequence of rabbit antibodies,” J. Biol. Chem. 214(1): 185 (1955).

    Google Scholar 

  150. R. Mage and E. A. Kabat, “The combining regions of the type III pneumococcus polysaccharide and homologous antibody,” Biochemistry 2(6): 1278 (1963).

    PubMed  CAS  Google Scholar 

  151. W.J. Mandy, M. K. Stambaugh, and A. Nisonoff, “Amino acid composition of univalent fragments of rabbit antibody,” Science 140(3569):901 (1963).

    PubMed  CAS  Google Scholar 

  152. E. Marier, C. A. Nelson, and C. Tanford, “The polypeptide chains of rabbit y -globulin and its papain-cleaved fragments,” Biochemistry 3(2):279 (1964).

    Google Scholar 

  153. G. Markus, A. L. Grossberg, and D. Pressman, “The disulfide bonds of rabbit γ -globulin and its fragments,” Arch. Biochem. Biophys. 96(1):63 (1962).

    PubMed  CAS  Google Scholar 

  154. E. Marler and D. Gitlin, “Comparison of the peptides released from human and rabbit γ2-globulins by enzymatic digestion,” Nature 198(4887): 1304 (1963).

    Google Scholar 

  155. C. Merryman and B. Benacerraf, “Studies on the structure of mouse antibodies,” Proc. Soc. Exp. Biol. Med. 114(2):372 (1963).

    PubMed  CAS  Google Scholar 

  156. H. Metzger, “Characterization of a human macroglobulin. V. A Waldenström macroglobulin with antibody activity, ” Proc. Nat. Acad. Sci. USA 57(5):1490 (1967).

    PubMed  CAS  Google Scholar 

  157. H. Metzger and M. Mannick, “Recombination of antibody polypeptide chains in the presence of antigen,” J. Exp. Med. 114(2):372 (1963).

    Google Scholar 

  158. H. Metzger and S.J. Singer, “Binding capacity of reductively fragmented antibodies to the 2,4-dinitrophenyl group,” Science 142(3593):674 (1963).

    PubMed  CAS  Google Scholar 

  159. H. Metzger, L. Wofsy, and S. J. Singer, “Affinity labeling of the active sites of antibodies to the 2,4-dinitrophenyl hapten,” Biochemistry 2(5): 979 (1963).

    PubMed  CAS  Google Scholar 

  160. H. Metzger, L. Wofsy, and S. J. Singer, “The participation of A and B polypeptide in the active sites of antibody molecules,” Proc. Nat. Acad. Sci. USA 51(4): 612 (1964).

    PubMed  CAS  Google Scholar 

  161. S. Mihaescu, “The heterogeneity of the polypeptide L chain rabbit IgG. Electrophoresis and Immunoelectrophoresis,” Rev. Roumaine Biochim. 4(3):193 (1967).

    CAS  Google Scholar 

  162. F. Miller and H. Metzger, “Characterization of a human macroglobulin. I. The molecular weight of its subunit,” J. Biol. Chem. 240(8):3325 (1965).

    PubMed  CAS  Google Scholar 

  163. C. Milstein, “Chemical structure of light chains,” Proc. Roy. Soc, Ser. B 166(1003):146 (1966).

    Google Scholar 

  164. C. Milstein, “Variations in the C-terminal half of immunoglobulin lambda chains,” Biochem. J. 104(2):28c (1967).

    CAS  Google Scholar 

  165. C. Milstein, “Variations in amino acid sequence near the disulfide bridges of Bence-Jones proteins,” Nature 209(5021):370 (1966).

    PubMed  CAS  Google Scholar 

  166. E. Mozes, J. B. Robbins, and M. Sela, “Heterogeneity of the light chains of rabbit immunoglobulin G fractions and of a series of antibodies directed towards antigens of differing complexity,” Immunochemistry 4(4):239 (1967).

    PubMed  CAS  Google Scholar 

  167. R. L. Nachman and R. L. Engle, “Gamma-globulin: unmasking of hidden antigenic sites on light chains,” Science 145(3628): 167 (1964).

    PubMed  CAS  Google Scholar 

  168. C. A. Nelson, “Isolation of a new intermediate in the papain cleavage of rabbit gamma-globulin,” J. Biol. Cherrf. 239(11):3727 (1964).

    CAS  Google Scholar 

  169. C. A. Nelson, M. E. Noelken, C. E. Buckley, C. Tanford, and R. L. Hill, “Tryptic hydrolysis of the inactive fragments of rabbit gamma-globulin in antibodies,” Federation Proc. 22(2):657 (1963).

    Google Scholar 

  170. C. A. Nelson, M. E. Noelken, C. E. Buckley, C. Tanford, and R. L. Hill, “Comparison of tryptic peptides from rabbit gamma-globulin and two specific rabbit antibodies,” Biochemistry 4(7):1418 (1965).

    CAS  Google Scholar 

  171. A. Nisonoff, “Resynthesis of precipitating antibody from univalent fragments,” Biochem. Biophys. Res. Commun. 3(5):466 (1960).

    PubMed  CAS  Google Scholar 

  172. A. Nisonoff and D. J. Dixon, “Evidence for linkage of univalent fragments of half-molecules of rabbit gamma-globulin by the same disulfide bond,” Biochemistry 3(9):1338 (1964).

    PubMed  CAS  Google Scholar 

  173. A. Nisonoff and W.J. Mandy, “Quantitative estimation of the hybridization of rabbit antibodies,” Nature 194(4826):355 (1962).

    PubMed  CAS  Google Scholar 

  174. A. Nisonoff, G. Markus, and F. C. Wissler, “Separation of univalent fragments of rabbit antibody by reduction of a single, labile disulfide bond,” Nature 189(4761):293 (1961).

    PubMed  CAS  Google Scholar 

  175. A. Nisonoff and J. L. Palmer, “Hybridization of half molecules of rabbit gamma-globulin,” Science 143(3604):376 (1964).

    PubMed  CAS  Google Scholar 

  176. A. Nisonoff and D. Pressman, “Studies on the combining site of anti-p-azobenzoate antibody. Loss of precipitating and binding capacities through different mechanisms on acetylation,” J. Immunol. 83(2): 138 (1959).

    CAS  Google Scholar 

  177. A. Nisonoff and M. M. Rivers, “Recombination of a mixture of univalent antibody fragments of different specificity, “Arch. Biochem. Biophys. 93(2):460 (1961).

    PubMed  CAS  Google Scholar 

  178. A. Nisonoff, F. C. Wissler, and L. N. Lipman, “Properties of the major component of a peptic digest of rabbit antibody,” Science 132(3441): 1770 (1960).

    PubMed  CAS  Google Scholar 

  179. A. Nisonoff, F. C. Wissler, L.N. Lipman, and D. L. Woernley, “Separation of univalent fragments from bivalent rabbit antibody molecule by reduction of disulfide bonds,” Arch. Biochem. Biophys. 89(2):230 (1960).

    PubMed  CAS  Google Scholar 

  180. A. Nisonoff, F. C. Wissler, and D. L. Woernley, “Mechanism of the formation of univalent fragments of rabbit antibody,” Biochem. Biophys. Res. Commun. 1(6):318 (1959).

    CAS  Google Scholar 

  181. A. Nisonoff, F. C. Wissler, and D. L. Woernley, “Properties of univalent fragments of rabbit antibody isolated by specific adsorption,” Arch. Biochem. Biophys. 88(2):241 (1960).

    PubMed  CAS  Google Scholar 

  182. A. Nisonoff and D. L. Woernley, “Effect of hydrolysis by papain on the combining sites on an antibody,” Nature 183(4671): 1325 (1959).

    PubMed  CAS  Google Scholar 

  183. M. E. Noelken and C. Tanford, “Unfolding and renaturation of a univalent anti-hapten antibody fragment,” J. Biol. Chem. 239(6):1828 (1964).

    PubMed  CAS  Google Scholar 

  184. C. Nolan and E. L. Smith, “Glycopeptides. III. Isolation and properties of glycopeptides from a bovine globulin of colostrum and from fraction II-3 of human globulin,” J. Biol. Chem. 237(2):453 (1962).

    PubMed  CAS  Google Scholar 

  185. “Notation for human immunoglobulin subclasses,” Bull. World Health Organ. 35(6): 953 (1966).

    Google Scholar 

  186. V. Nussenzweig and B. Benacerraf, “Studies on the properties of fragments of guinea pig γ 1 and γ2 antibodies obtained by papain digestion and mild reduction,” J. Immunol. 93(6):1008 (1964).

    PubMed  CAS  Google Scholar 

  187. V. Nussenzweig and B. Benacerraf, “Electrophoretic patterns at acid and alkaline pH of reduced guinea pig 7 S gamma-globulin and antihapten antibodies of different specificities,” Intern. Arch. Allergy Appl. Immunol. 27(4): 193 (1965).

    CAS  Google Scholar 

  188. V. Nussenzweig, E. C. Franklin, and B. Benacerraf, “Immunologic properties of products obtained by mild reduction of human and guinea pig γ-globulins,” Immunol. 93(6): 1015 (1964).

    CAS  Google Scholar 

  189. D.E. Olins and G. M. Edelman, “The antigenic structure of the polypeptide chains of human γ-globulin,” J. Exp. Med. 116(5):635 (1962).

    PubMed  CAS  Google Scholar 

  190. D.E. Olins and G. M. Edelman, “Reconstitution of 7 S molecules from L and H polypeptide chains of antibodies and γ-globulins, “J. Exp. Med. 119(5):789 (1964).

    PubMed  CAS  Google Scholar 

  191. K. Onoue, Y. Yagi, P. Stelos, and D. Pressman, “Antigen-binding activity of 6 S subunits of β 2-macroglobulin antibody,” Science 146(3642):404 (1964).

    PubMed  CAS  Google Scholar 

  192. E. F. Osserman and K. Takatsuki, “Clinical and immunochemical studies of four cases of heavy (Hγ2) chain disease,” Am. J. Med. 37(3):351 (1964).

    PubMed  CAS  Google Scholar 

  193. J. Oudin, “On the associated state of rabbit allotypes, the existence of rabbit antibody molecules against two allotypes, and the dissociation of human γ -globulin antigens into smaller molecules,” Biochem. Biophys. Res. Commun. 5(5):358(1961).

    CAS  Google Scholar 

  194. R. H. Pain, “The molecular weight of the peptide chains of γ-globulin,” Biochem. J. 88(2):234 (1963).

    PubMed  CAS  Google Scholar 

  195. J. L. Palmer, W.J. Mandy, and A. Nisonoff, “Heterogeneity of rabbit antibody and its subunits,” Proc. Nat. Acad. Sci. USA 48(1):49 (1962).

    PubMed  CAS  Google Scholar 

  196. J. L. Palmer and A. Nisonoff, “Reduction and reoxidation of a critical disulfide bond in the rabbit antibody molecule,” J. Biol. Chem. 238(7):2393 (1963).

    CAS  Google Scholar 

  197. J. L. Palmer and A. Nisonoff, “Dissociation of rabbit γ-globulin into half molecules after reduction of one labile disulfide bond,” Biochemistry 3(6):863 (1964).

    PubMed  CAS  Google Scholar 

  198. J. L. Palmer, A. Nisonoff, and K. E. Van Holde, “Dissociation of rabbit γ -globulin into subunits. Reduction and acidification,” Proc. Nat. Acad. Sci. USA 50(2):314 (1963).

    PubMed  CAS  Google Scholar 

  199. I.A. Parfentjev, US Patents 2,065,196 (1936), 2,123,198 (1938), 2,175,000 (1939), cit. R. R. Porter, Plasma Proteins, 1:257 (1960).

    Google Scholar 

  200. J. F. Pechere, G. H. Dixon, R. H. Maybury, and H. Neurath, “Cleavage of disulfide bonds in trypsinogen and α-chymotrypsinogen,” J. Biol. Chem. 233(6):1364(1958).

    PubMed  CAS  Google Scholar 

  201. M. L. Petermann, “The action of papain on beef serum Pseudoglobulin and on diphtheria antitoxin,” J. Biol. Chem. 144(3):607 (1942).

    CAS  Google Scholar 

  202. M. L. Petermann, “The splitting of human γ-globulin antibodies by papain and bromelin,” J. Am. Chem. Soc. 68(1):106 (1946).

    PubMed  CAS  Google Scholar 

  203. P.J. Piggot and E. M. Press, “Cyanogen bromide cleavage and partial sequence of the heavy chain of a pathological immunoglobulin G,” Biochem. J. 104(2):616 (1967).

    PubMed  CAS  Google Scholar 

  204. C.G. Pope and M. Healey, “The preparation of diphtheria antitoxin in a state of high purity,” Brit. J. Exp. Pathol. 20(3):213 (1939).

    CAS  Google Scholar 

  205. R. R. Porter, “The formation of a specific inhibitor by hydrolysis of rabbit antiovalbumin,” Biochem. J. 46(4):479 (1950).

    PubMed  CAS  Google Scholar 

  206. R. R. Porter, “The structure of the heavy chain of immunoglobulin and its revevance to the nature of antibody-combining site,” Biochem. J. 105(2):417 (1967).

    PubMed  CAS  Google Scholar 

  207. R. R. Porter, “The hydrolysis of rabbit γ-globulin and its antibodies with crystalline papain,” Biochem. J. 73(1):119 (1959).

    PubMed  CAS  Google Scholar 

  208. R. R. Porter, “The structure of γ-globulins and antibodies,” in: Basic Problems in Neoplastic Disease, Columbia University Press, New York (1962), p. 177.

    Google Scholar 

  209. R. R. Porter, “The structure of antibodies,” Sci. Am. 217(4):81 (1967).

    PubMed  CAS  Google Scholar 

  210. R. R. Porter and E. M. Press, “Immunochemistry,” Ann. Rev. Biochem. 31:625 (1962).

    PubMed  CAS  Google Scholar 

  211. M. D. Poulik, “Ffc fragment of immunoglobulins,” Nature 210(5032):133 (1966).

    PubMed  CAS  Google Scholar 

  212. M. D. Poulik, “Heterogeneity of L(B) chains of γ -globulins,” Nature 202(4938):1174(1964).

    PubMed  CAS  Google Scholar 

  213. M. D. Poulik and G. M. Edelman, “Comparison of reduced alkylated derivatives of some myeloma globulins and Bence-Jones proteins,” Nature 191(4795):1274(1961).

    PubMed  CAS  Google Scholar 

  214. M. D. Culik and J. Schuster, “Heterogeneity of H chains of myeloma proteins: susceptibility to papain and trypsin,” Nature 204(4958):577 (1964).

    Google Scholar 

  215. J. Prahl, “Enzymic degradation of the Fc fragment of rabbit immunoglobulin IgG,” Biochem. J. 104(2):647 (1967).

    PubMed  CAS  Google Scholar 

  216. E. M. Press, “The amino acid sequence of the N -terminal 84 residues of a human heavy chain of immunoglobulin G (Daw),” Biochem. J. 104(2):30c (1967).

    CAS  Google Scholar 

  217. D. Pressman, A. L. Grossberg, O. Roholt, P. Stelos, and Y. Yagi, “The chemical nature of antibody molecules and their combining sites,” Ann. N. Y. Acad. Sci. 103(582) (1963).

    Google Scholar 

  218. D. Pressman, A. Nisonoff, and G. Radzimski, “Specific anion effects with anti-benzoate antibody,” J. Immunol. 86(1):35 (1961).

    PubMed  CAS  Google Scholar 

  219. D. Pressman and G. Radzimski, “Increased precipitability of antibody as a result of iodination,” J. Immunol. 89(3):367 (1962).

    PubMed  CAS  Google Scholar 

  220. D. Pressman and O. Roholt, “Isolation of peptides from an antibody site,” Proc. Nat. Acad. Sci. USA 47(10):1606 (1961).

    PubMed  CAS  Google Scholar 

  221. D. Pressman, P. Stelos, and A. Grossberg, “Retention of rabbit antibody activity during acetylation,” J. Immunol. 86(4):452 (1961).

    PubMed  CAS  Google Scholar 

  222. D. Pressman and L. A. Sternberger, “The nature of the combining sites of antibodies. The specific protection of the combining site by hapten during iodination,” J. Immunol. 66(5):609 (1951).

    PubMed  CAS  Google Scholar 

  223. F. W. Putnam et al., “The cleavage of rabbit γ-globulin by papain,” J. Biol. Chem. 237(3):717 (1962).

    PubMed  CAS  Google Scholar 

  224. F. W. Putnam, “Structural relationships among normal human γ-globulin myeloma globulins and Bence—Jones proteins,” Biochem. Biophys. Acta 63(3):539(1952).

    Google Scholar 

  225. F. W. Putnam and C. W. Easley, “Structural studies of the immunoglobulins. I. The tryptic peptides of Bence-Jones proteins,” J. Biol. Chem. 240(4): 1626 (1965).

    PubMed  CAS  Google Scholar 

  226. F. W. Putnam, K. Titani, M. Wikler, and T. Shinoda, “Structure and evolution of kappa and lambda light chains,” Cold Spring Harbor Symp. Quant. Biol., p. 6(1967).

    Google Scholar 

  227. F. W. Putnam, C. W. Easley, and L. T. Lynn, “Site of cleavage of γ-globulins by papain,” Biochim. Biophys. Acta 58(2):279 (1962).

    PubMed  CAS  Google Scholar 

  228. J. Reynek, O. Kotynek, and J. Kostka, “Contribution to the structural characterization of γ -globulin from pig colostrum,” Folia Microbiol. 10(6):327 (1965).

    Google Scholar 

  229. R. A. Reisfield and P.A. Small, “Electrophoretic heterogeneity of polypeptide chains of specific antibodies,” Science 152(3726): 1253 (1966).

    Google Scholar 

  230. O. Roholt, A. Grossman, K. Onoue, and D. Pressman, “Relative contributions of H and L chains to the binding site of antibody molecules,” Abstr. VI Intern. Biochem. Congr. New York 2:176 (1964).

    Google Scholar 

  231. O. Roholt, K. Onoue, and D. Pressman, “Specific combination of H and L chains of rabbit γ-globulins,” Proc. Nat. Acad. Sci. USA 51(2):173 (1964).

    PubMed  CAS  Google Scholar 

  232. O. Roholt and D. Pressman, “A discontinuous heterogeneity of heavy chains of rabbit antibody molecules,” Science 153(3741):1257 (1966).

    PubMed  CAS  Google Scholar 

  233. O. A. Roholt, G. Radzimski, and D. Pressman, “Polypeptide chains of antibody: effective binding sites require specificity in combination,” Science 147(3658):613 (1965).

    PubMed  CAS  Google Scholar 

  234. O. A. Roholt, G. Radzimski, and D. Pressman, “Antibody combining site: The B polypeptide chain,” Science 141(3582):726 (1963).

    PubMed  CAS  Google Scholar 

  235. O.A. Roholt, G. Radzimski, and D. Pressman, “Preferential recombination of antibody chains to form effective binding sites,” J. Exp. Med. 122(4):785 (1965).

    PubMed  CAS  Google Scholar 

  236. O. A. Roholt, G. Radzimski, and D. Pressman, “Specificity in the combination of Fd fragments with L-chains to form hapten-binding sites,” J. Exp. Med. 123(5):921 (1966).

    PubMed  CAS  Google Scholar 

  237. O. A. Roholt, G. Radzimski, and D. Pressman, “Recovery of activity from inactive hybrids of H and L chains,” J. Exp. Med. 125(1): 191 (1967).

    PubMed  CAS  Google Scholar 

  238. O. Roholt, A Shaw, and D. Pressman, “Preferential recombination of antibody fragments as shown by paired label studies,” Nature 196(4856):773 (1962).

    PubMed  CAS  Google Scholar 

  239. J. H. Rockey, N. R. Klinman, and F. Karush, “Equine antihapten antibody. I. 7 S β -2A- and 10 S γ-globulin components of purified anti-β -lactoside antibody,” J. Exp. Med. 120(4):589 (1964).

    PubMed  CAS  Google Scholar 

  240. H. J. Sage, C. F. Deutsch, G. D. Fasman, and L. Levine, “The serological specificity of the polyalanine immune system,” Immunochemistry 1(2):133 (1964).

    PubMed  CAS  Google Scholar 

  241. I. Schechter and M. Sela, “Combining sites of antibodies to L-alanine and D-alanine peptide determinants,” Biochim. Biophys. Acta 104(1):298 (1965).

    PubMed  CAS  Google Scholar 

  242. J. Schechter and A. Berger, “On the size of the active site in proteases. I. Papain,” Biochem. Biophys. Res. Commun. 27(2):157 (1967).

    PubMed  CAS  Google Scholar 

  243. R. E. Schrohenloher, “The degradation of human γ-globulin by trypsin,” Arch. Biochem. Biophys. 101(3):456 (1963).

    PubMed  CAS  Google Scholar 

  244. R. E. Schrohenloher, H. G. Kunkel, and T. B. Tomasi, “Activity of dissociated and reassociated 19 S anti-γ-globulins,” J.Exp. Med. 120(6):1215 (1964).

    PubMed  CAS  Google Scholar 

  245. P. H. Schur and G. D. Christian, “The role of disulfide bonds in the complement-fixing and precipitating properties of 7 S rabbit and sheep antibodies,” J. Exp. Med. 120(4):531 (1964).

    PubMed  CAS  Google Scholar 

  246. J. H. Schwartz and G. M. Edelman, “Comparisons of Bence-Jones proteins and L polypeptide chains of myeloma globulins after hydrolysis with trypsin,” J. Exp. Med. 118(1):41 (1963).

    PubMed  CAS  Google Scholar 

  247. M. Sela, D. Givol, and E. Mozes, “Resolution of rabbit γ -globulin into two fractions by chromatography on diethylaminoethyl-sephadex,” Biochem. Biophys. Acta 73:649 (1963).

    Google Scholar 

  248. M. Sela, “Immunological studies with synthetic polypeptides,” Advan. Immunol. 5:30 (1967).

    Google Scholar 

  249. H. G. Scijen and M. Gruber, “Structure of γ -globulins and antibodies,” J. Mol. Biol. 7(2):209(1963).

    Google Scholar 

  250. J. Sjöquist and M. H. Vaughn, “Heterogeneity of H and L chains of normal

    Google Scholar 

  251. and myeloma yG-globulin,” J. Mol. Biol. 20(3):527 (1966).

    Google Scholar 

  252. S. J. Singer and R. F. Doolittle, “Antibody active sites and immunoglobulin

    Google Scholar 

  253. molecules,” Science 153(3731):13 (1966).

    Google Scholar 

  254. F. Skvaril, “Changes in outdated human γ-globulin preparations,” Nature 185(4711):475 (1960).

    PubMed  CAS  Google Scholar 

  255. F. Skvaril, “Inhibitions of spontaneous splitting of γ-globulin preparations with ε -aminocaproic acid,” Nature 196(4853):481 (1962).

    PubMed  CAS  Google Scholar 

  256. F. Skvaril and J. Radl, “The fragmentation of human IgD during storage,” Clin. Chim. Acta 15:544 (1967).

    PubMed  CAS  Google Scholar 

  257. F. Skvaril, V. Brummelova, and F. Franek, “Isolation of kappa and lambda chains from normal human γ G-globulin by ion-exchange chromatography,” Biochim. Biophys. Acta 140(2):371 (1967).

    PubMed  CAS  Google Scholar 

  258. A. Small, J. E. Kenn, and M. E. Lamm, “Polypeptide chains of rabbit γ -globulin,” Science 142(3590):393 (1963).

    PubMed  CAS  Google Scholar 

  259. P. A. Small and M. E. Lamm, “Polypeptide chain structure of rabbit immunoglobulins. I. γ G-immunoglobulin,” Biochemistry 5(1):259 (1966).

    PubMed  CAS  Google Scholar 

  260. D.S. Smyth and S. Utsumi, “Structure of the hinge region in rabbit immunoglobulin G,” Nature 216(5113):332 (1967).

    PubMed  CAS  Google Scholar 

  261. S. R. Stein, J. L. Palmer, and A. Nisonoff, “Reformation of interchain bonds linking half-molecules of rabbit γ -globulin,” J. Biol. Chem. 239(9):2872 (1964).

    PubMed  CAS  Google Scholar 

  262. A. G. Steinberg, “Genetic variations in human immunoglobulins: the Gm and Inv types,” in: Symposium on immunogenetics, Lippincott, Philadelphia (1967).

    Google Scholar 

  263. P. Stelos and D. Pressman, “Papain digestion of antigen-antibody precipitates,” J. Biol. Chem. 237(12):3679 (1962).

    PubMed  CAS  Google Scholar 

  264. P. Stelos, G. Radzimski, and D. Pressman, “Heterogeneity of rabbit antibody fragments,” J. Immunol. 88(5):572 (1962).

    PubMed  CAS  Google Scholar 

  265. P. Stelos, Y. Yagi, and D. Pressman, “Multiple discrete components of the univalent fragments of rabbit antibody,” J. Immunol. 93(1): 106 (1964).

    PubMed  CAS  Google Scholar 

  266. D. Stolinsky and H. Fudenberg, “On the univalent fragments of human 7 S γ-globulin, Nature 200(4909):856 (1963).

    PubMed  CAS  Google Scholar 

  267. J. M. Swan, “Thiols, disulfides, and thiosulphates: some new reactions and possibilities in peptide and protein chemistry,” Nature 180(4587):643 (1957).

    CAS  Google Scholar 

  268. K. Takatsuki and E. F. Osserman, “Structural difference between two types of “heavy chain” disease proteins and myeloma globulins of corresponding types,” Science 145(3631):499 (1964).

    PubMed  CAS  Google Scholar 

  269. M. Tan and W. V. Epstein, “Purification of γ-globulin fragments by gel filtration,” Science 139(3549):53 (1963).

    PubMed  CAS  Google Scholar 

  270. W. D. Terry, “Subclasses of human IγG molecules differing in heterologous skin sensitizing properties,” Proc. Soc. Exp. Biol. Med. 117(3):901 (1964).

    PubMed  CAS  Google Scholar 

  271. W. D. Terry and J. L. Fahey, “Subclasses of human γ-globulin based on differences in the heavy polypeptide chains,” Science 146(3642):400 (1964).

    PubMed  CAS  Google Scholar 

  272. K. Titani and F. W. Putnam, “Immunoglobulin structure: amino and carboxyl terminal peptides of type I Bence-Jones proteins,” Science 147(3663): 1304 (1965).

    PubMed  CAS  Google Scholar 

  273. K. Titani, M. Wikler, and F. W. Putnam, “Evolution of immunoglobulins’ structural homology of kappa and lambda Bence-Jones proteins,” Science 155(3764):828 (1967).

    PubMed  CAS  Google Scholar 

  274. H. Ungar-Waron, J. C. Jaton, and M. Sela, “Action of papain on normal rabbit immunoglobulin M,” Biochim. Biophys. Acta 140(3):542 (1967).

    PubMed  CAS  Google Scholar 

  275. S. Utsumi and F. Karush, “Peptic fragmentation of rabbit γ G-immunoglobulin,” Biochemistry 4(9):1766 (1965).

    CAS  Google Scholar 

  276. S. Utsumi and F. Karush, “The subunits of purified rabbit antibody,” Biochemistry 3(9):1766 (1965).

    Google Scholar 

  277. S. Utsumi and F. Karush, “Chemical characterization of the peptic fragments of rabbit γ G- immunoglobulin,” Biochemistry 6(8):2313 (1967).

    PubMed  CAS  Google Scholar 

  278. M. H. Winkler, “On the structure of specific antibody site,” J. Theoret. Biol. 4(3):237 (1963).

    CAS  Google Scholar 

  279. P. L. Whitney and C. Tanford, “Recovery of specific activity after complete unfolding and reduction of an antibody fragment,” Proc. Nat. Acad. Sci. USA 53(3):524(1965).

    PubMed  CAS  Google Scholar 

  280. S. F. Velick, C. Parker, and H.N. Eisen, “Excitation energy transfer and the quantitative study of the antibody hapten reaction,” Proc. Nat. Acad. Sci. USA 46(11): 1470 (1960).

    PubMed  CAS  Google Scholar 

  281. R. C. Weir and R. R. Porter, “The antigen-binding capacity of the peptide chains of horse antibodies,” Biochem. J. 100(1):69 (1966).

    PubMed  CAS  Google Scholar 

  282. R. C. Williams, “Heterogeneity of L -chain sites on Bence—Jones proteins reacting with anti-γ -globulin factors,” Proc. Nat. Acad. Sci. USA 52(1): 60 (1964).

    PubMed  Google Scholar 

  283. L. Wofsy, H. Metzger, and S. J. Singer, “Affinity labeling — a general method for labeling the active sites of antibody and enzyme molecules,” Biochemistry 1:1031 (1962).

    PubMed  CAS  Google Scholar 

  284. L. Wofsy and S. J. Singer, “Effects of the amidination reaction on antibody activity and on the physical properties of some proteins,” Biochemistry 2(1): 104 (1963).

    PubMed  CAS  Google Scholar 

  285. L. Wofsy, N. R. Klinman, and F. Karush, “Affinity labeling of equine anti-β-lactoside antibodies,” Biochemistry 6(7):1988 (1967).

    PubMed  CAS  Google Scholar 

  286. T. J. Yoo, O. A. Roholt, and D. Pressman, “Specific binding activity of isolated light chains of antibodies,” Science 157(3789):707 (1967).

    PubMed  CAS  Google Scholar 

  287. J. Zikan, B. Skvarova, and J. Rejnek, “Two structurally different types of rabbit light chains,” Folia Microbiol. 12(2):162 (1967).

    CAS  Google Scholar 

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Nezlin, R.S. (1970). The Structure of Antibodies. In: Biochemistry of Antibodies. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-1791-3_4

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