Skip to main content
The Journal of Experimental Medicine logoLink to The Journal of Experimental Medicine
. 1963 Jan 31;117(2):213–230. doi: 10.1084/jem.117.2.213

TWO MAJOR TYPES OF NORMAL 7S γ-GLOBULIN

Mart Mannik 1, Henry G Kunkel 1
PMCID: PMC2137606  PMID: 19867222

Abstract

Normal 7S human γ-globulin was found to contain two fundamental antigenic groups of molecules. The group 1 molecules of normal γglobulin correspond antigenically to group 1 multiple myeloma proteins and Bence Jones proteins; and group 2 molecules of normal γ-globulin correspond antigenically to group 2 multiple myeloma proteins and Bence-Jones proteins. Among pooled human Fr II and several individual γ-globulin preparations, approximately 60 per cent of molecules belong to group 1 and approximately 30 per cent of molecules to group 2 in this classification. The possible existence of a third minor antigenic group, constituting about 10 per cent, is discussed. Antisera to Bence Jones proteins of antigenic group 1 and group 2, in conjunction with I-131-labeled 7S γ-globulin proved to be the most useful system for defining the antigenic groups of normal γ-globulin. The group-specific antigenic determinants of normal 7S γ-globulin molecules were located on the S fragments of these proteins.

Full Text

The Full Text of this article is available as a PDF (961.3 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. ASKONAS B. A., HUMPHREY J. H. The distribution of antigenic groupings on mouse gamma-globulin molecules. Nature. 1961 Jun 24;190:1177–1178. doi: 10.1038/1901177a0. [DOI] [PubMed] [Google Scholar]
  2. AUGUSTIN R., HAYWARD B. J. Immunochemical studies of human serum proteins. Antigenic inhomogeneities of the gamma globulins, their subunits and number of determinants and their relation to a Waldenstrom macroglobulin. Immunology. 1961 Oct;4:450–472. [PMC free article] [PubMed] [Google Scholar]
  3. DRAY S. Three gamma-globulins in normal human serum revealed by monkey precipitins. Science. 1960 Nov 4;132(3436):1313–1314. doi: 10.1126/science.132.3436.1313. [DOI] [PubMed] [Google Scholar]
  4. EDELMAN G. M., HEREMANS J. F., HEREMANS M. T., KUNKEL H. G. Immunological studies of human gamma-globulin. Relation of the precipitin lines of whole gamma-globulin to those of the fragments produced by papain. J Exp Med. 1960 Jul 1;112:203–223. doi: 10.1084/jem.112.1.203. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. FAHEY J. L., LAWLER S. D. Gm factors in normal gamma-globulin fractions, myeloma proteins, and macroglobulins. J Natl Cancer Inst. 1961 Nov;27:973–981. [PubMed] [Google Scholar]
  6. FRANKLIN E. C., FUDENBERG H., MELTZER M., STANWORTH D. R. The structural basis for genetic variations of normal human gamma-globulins. Proc Natl Acad Sci U S A. 1962 Jun 15;48:914–922. doi: 10.1073/pnas.48.6.914. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. GRABAR P. The use of immunochemical methods in studies on proteins. Adv Protein Chem. 1958;13:1–33. doi: 10.1016/s0065-3233(08)60597-5. [DOI] [PubMed] [Google Scholar]
  8. HARBOE M., OSTERLAND C. K., KUNKEL H. G. Localization of two genetic factors to different areas of gamma-globulin molecules. Science. 1962 Jun 15;136(3520):979–980. doi: 10.1126/science.136.3520.979. [DOI] [PubMed] [Google Scholar]
  9. HARBOE M., OSTERLAND C. K., MANNIK M., KUNKEL H. G. Genetic characters of human gamma-globulins in myeloma proteins. J Exp Med. 1962 Nov 1;116:719–738. doi: 10.1084/jem.116.5.719. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. KORNGOLD L. Abnormal plasma components and their significance in disease. Ann N Y Acad Sci. 1961 Aug 31;94:110–130. doi: 10.1111/j.1749-6632.1961.tb35536.x. [DOI] [PubMed] [Google Scholar]
  11. KORNGOLD L., VAN LEEUWEN G. The use of cross-reacting antiserums for the study of antigenic heterogeneity of mammalian gama2-globulins. Int Arch Allergy Appl Immunol. 1961;19:271–283. doi: 10.1159/000229217. [DOI] [PubMed] [Google Scholar]
  12. KUNKEL H. G. Zone electrophoresis. Methods Biochem Anal. 1954;1:141–170. doi: 10.1002/9780470110171.ch6. [DOI] [PubMed] [Google Scholar]
  13. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  14. MASOUREDIS S. P., MELCHER L. R., KOBLICK D. C. Specificity of radioiodinated (I131) immune globulin as determined by quantitative precipitin reaction. J Immunol. 1951 Mar;66(3):297–302. [PubMed] [Google Scholar]
  15. Mannik M., Kunkel H. G. CLASSIFICATION OF MYELOMA PROTEINS, BENCE JONES PROTEINS, AND MACROGLOBULINS INTO TWO GROUPS ON THE BASIS OF COMMON ANTIGENIC CHARACTERS. J Exp Med. 1962 Nov 30;116(6):859–877. doi: 10.1084/jem.116.6.859. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. PORTER R. R. The hydrolysis of rabbit y-globulin and antibodies with crystalline papain. Biochem J. 1959 Sep;73:119–126. doi: 10.1042/bj0730119. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. PUTNAM F. W., UDIN B. Proteins in multiple myeloma. I. Physicochemical study of serum proteins. J Biol Chem. 1953 Jun;202(2):727–743. [PubMed] [Google Scholar]
  18. SLATER R. J. The serum gamma-globulins defined by electrophoretic and immunologic analyses. Arch Biochem Biophys. 1955 Nov;59(1):33–44. doi: 10.1016/0003-9861(55)90460-4. [DOI] [PubMed] [Google Scholar]

Articles from The Journal of Experimental Medicine are provided here courtesy of The Rockefeller University Press

RESOURCES