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Original Articles

Structural Characteristics of Human Immunoglobulins

, M.D.
Pages 133-143 | Published online: 18 Apr 2016

REFERENCES

  • Cohen, S. and Porter, R. R.: Structure and biological activity of immunoglobulins. Advances Immun 4: 287, 1964.
  • Fahey, J. L.: Antibodies and immunoglobulins. I. Structure and function. JAMA 194: 183, 1965.
  • Franklin, E. C.: Immune globulins: Their structure and function and some techniques for their isolation. Progr Allerg 8: 58, 1964.
  • Fudenberg, H. H.: The immune globulins. Ann Rev Microbiol 19: 301, 1965.
  • Nlsonoff, A. and Thorbecke, G. J.: Immuno- chemistry. Ann Rev Biochem 33: 355, 1964.
  • Gltlin, D.: Current aspects of the structure, function and genetics of the immunoglobulins. Ann Rev Med 17: 1, 1966.
  • Heremans, J. F.: Personal communication.
  • Ishizaka, K., Ishizaka, T. and Hornbrook, M.: Physico-chemical properties of human reaginic antibody. IV. Presence of a unique immunoglobulin as a carrier of reaginic activity. J Immun 97: 75, 1966.
  • Edelman, G. M. and Benacerraf, B.: On structural and functional relations between antibodies and proteins of gamma-system. Proc Nat Acad Sci USA 48: 1035, 1962.
  • Fleischman, J. B., Porter, R. R. and Press, E. M.: Arrangement of peptide chains in γ-globulin. Biochem J 88: 220, 1963.
  • Porter, R. R.: The hydrolysis of rabbit γ-globulin and antibodies with crystalline papain. Biochem J 73: 119, 1959.
  • Nisonoff, A., Wissler, F. C., Lipman, L. N. and Woernley, D. L.: Separation of univalent fragments from the bivalent rabbit antibody molecule by reduction of disulfide bonds. Arch Biochem 89: 230, 1960.
  • Franek, F. and Nezlin, R. S.: Recovery of antibody combining activity by interaction of different peptide chains isolated from purified horse antitoxins. Folia Microbiol 8: 128, 1963.
  • Goodman, J. W. and Donch, J. J.: Phage-neu-tralizing activity in light polypeptide chains of rabbit antibody. Immunochemistry 2: 351, 1965.
  • Mannik, M. and Kunkel, H. G.: Two major types of 7S γ-globulin. J Exp Med 117: 213, 1963.
  • Fahey, J. L.: Structural basis of differences between type I and type II human gamma-globulin molecules. J Immun 91: 448, 1963.
  • Grey, H. M. and Kunkel, H. G.: H chain subgroups of myeloma proteins and normal 7S γ-globulin. J Exp Med 120: 253, 1964.
  • Terry, W. D. and Fahey, J. L.: Subclasses of human γ2-globulin based on differences in heavy polypeptide chains. Science 146: 400, 1964.
  • Terry, W. D.: Skin-sensitizing activity related to γ-polypeptide chain characteristics of human IgG. J Immun 95: 1041, 1965.
  • Harboe, M., Deverill, J. and Godal, H. G: Antigenic heterogeneity of Waldenström type γM- globulins. Scand J Haemat 2: 137, 1965.
  • Kunkel, H. G. and Prendergast, R. A.: Subgroups of γA immune globulins. Proc Soc Exp Biol Med 122: 910, 1966.
  • Vaerman, J. P. and Heremans, J. F.: Subclasses of human IgA based on differences in the alpha polypeptide chains. Science 153: 647, 1966.
  • Terry, W. D. and Robert, M. S.: Antigenic heterogeneity of human immunoglobulin A proteins. Science (in press).
  • Steinberg, A. G.: Progress in the study of genetically determined human gamma globulin types (the Gm and Inv groups). Progr Med Genet 2: 1, 1962.
  • Steinberg, A. G.: Genetic variations in human immunoglobulins: The Gm and Inv types. In Greenwalt, T. J. (Editor): Symposium on Immunogenetics. Philadelphia, J. B. Lippincott Company (in press).
  • Kunkel, H. G., Allen, J. C., Grey, H. M., Mȧrtensson, L. and Grubb, R.: A relationship between the H chain groups of 7S γ-globulin and the Gm system. Nature 203: 413, 1964.
  • Mȧrtensson, L. and Kunkel, H. G.: Distribution among the γ-globulin molecules of different genetically determined antigenic specificities in the Gm system. J Exp Med 122: 799–811 (October 1) 1965.
  • Terry, W. D., Fahey, J. L. and Steinberg, A. G.: Gm and Inv factors in subclasses of human IgG. J Exp Med 122: 1087, 1965.
  • Kunkel, H. G., Yount, W. J. and Litwin, S. D.: Genetically determined antigen of the Ne subgroup of γ-globulin: Detection by precipitin analysis. Science 154: 1041, 1966.
  • . Cohen, S.: Properties of the peptide chains of normal and pathological human γ-globulins. Biochem J 89: 334, 1963.
  • Cebra, J. J. and Small, P. A.: Polypeptide chain structure of rabbit immunoglobulins. III. Secretory γA from colostrum. (To be published.)
  • Tomasi, T. B., Tan, E. M., Solomon, A. and Prendergast, R. A.: Characteristics of an immune system common to certain external secretions. J Exp Med 121: 101, 1965.
  • South, M., Cooper, M. D., Wollheim, F. A., Hong, R. and Good, R. A.: The IgA system. I. Studies of the transport and immunochemistry of IgA in the saliva. J Exp Med 123: 615, 1966.
  • Miller, F. and Metzger, H.: Characterization of a human macroglobulin. I. The molecular weight of its subunit. J Biol Chem 240: 3325, 1965.
  • Rowe, D. S. and Fahey, J. L.: New class of human immunoglobulins: I. Unique myeloma protein. J Exp Med 121: 171, 1965.
  • Korngold, L. and Lipari, R.: Multiple myeloma proteins. III. The antigenic relationship of Bence Jones proteins to normal gamma-globulin and multiple-myeloma serum proteins. Cancer 9: 262, 1956.
  • Milstein, C.: Disulphide bridges and dimers of Bence-Jones protein. J Molec Biol 9: 836–838 (September) 1964.
  • Hilschmann, N. and Craig, L. C.: Amino acid sequence studies with Bence-Jones proteins. Proc Nat Acad Sci USA 53: 1403, 1965.
  • Titani, K., Whitley, E. and Putnam, F. W.: Immunoglobulin structure: Variation in the sequence of Bence Jones proteins. Science 152: 1513, 1966.
  • Frangione, B. and Franklin, E. C.: Structural studies of human immunoglobulins. J Exp Med 122: 1, 1965.
  • Whitney, P. L. and Tanford, C.: Properties of the soluble product obtained from reoxidation of reduced fragment I from rabbit 7S γ-immunoglobulin. J Biol Chem 240: 4271, 1965.

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