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. 1965 Jul 1;122(1):1–10. doi: 10.1084/jem.122.1.1

STRUCTURAL STUDIES OF HUMAN IMMUNOGLOBULINS

DIFFERENCES IN THE FD FRAGMENTS OF THE HEAVY CHAINS OF G MYELOMA PROTEINS

Blas Frangione 1, Edward C Franklin 1
PMCID: PMC2138036  PMID: 14325471

Abstract

1. Comparison of peptide maps of the Fc fragments of normal G immunoglobulins and 11 G myeloma proteins of the We (b) type showed them to be very similar except for differences associated with the Gm type. Some additional differences were noted, however, in the Fc fragments of three Vi (c) myeloma proteins. 2. Peptide maps of heavy chains from the same G myeloma proteins differed from each other and from normal heavy chains. In general, the myeloma chains contained a larger number of well defined spots; some of these were common to normal heavy chains while others were unique to each protein. Others, present in normal heavy chains, were lacking in the myeloma proteins. 3. Comparison of the heavy chains and Fc fragments from the same protein suggests that much of the variability of different myeloma proteins and, presumably, antibodies resides in the Fd fragment. 4. Further support for this is given by the finding that the antigenic specificity of 3 myeloma proteins also appeared to reside in the Fd fragments.

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Selected References

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

  1. COHEN S. PROPERTIES OF THE PEPTIDE CHAINS OF NORMAL AND PATHOLOGICAL HUMAN GAMMA GLOBULINS. Biochem J. 1963 Nov;89:334–341. doi: 10.1042/bj0890334. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. EDELMAN G. M., BENACERRAF B., OVARY Z., POULIK M. D. Structural differences among antibodies of different specificities. Proc Natl Acad Sci U S A. 1961 Nov 15;47:1751–1758. doi: 10.1073/pnas.47.11.1751. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. EDELMAN G. M., OLINS D. E., GALLY J. A., ZINDER N. D. RECONSTITUTION OF IMMUNOLOGIC ACTIVITY BY INTERACTION OF POLYPEPTIDE CHAINS OF ANTIBODIES. Proc Natl Acad Sci U S A. 1963 Oct;50:753–761. doi: 10.1073/pnas.50.4.753. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. EDELMAN G. M., POULIK M. D. Studies on structural units of the gamma-globulins. J Exp Med. 1961 May 1;113:861–884. doi: 10.1084/jem.113.5.861. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. FAHEY J. L. CONTRIBUTION OF GAMMA-GLOBULIN SUBUNITS TO ELECTROPHORETIC HETEROGENEITY: IDENTIFICATION OF A DISTINCTIVE GROUP OF 6.6S GAMMA-MYELOMA PROTEINS. Immunochemistry. 1964 Jun;1:121–131. doi: 10.1016/0019-2791(64)90076-x. [DOI] [PubMed] [Google Scholar]
  6. FEINSTEIN A., GELL P. G., KELUS A. S. IMMUNOCHEMICAL ANALYSIS OF RABBIT GAMMA-G.OBULIN ALLOTYPES. Nature. 1963 Nov 16;200:653–654. doi: 10.1038/200653a0. [DOI] [PubMed] [Google Scholar]
  7. FLEISCHMAN J. B., PAIN R. H., PORTER R. R. Reduction of gamma-globulins. Arch Biochem Biophys. 1962 Sep;Suppl 1:174–180. [PubMed] [Google Scholar]
  8. FLEISCHMAN J. B., PORTER R. R., PRESS E. M. THE ARRANGEMENT OF THE PEPTIDE CHAINS IN GAMMA-GLOBULIN. Biochem J. 1963 Aug;88:220–228. doi: 10.1042/bj0880220. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. FRANEK F., NEZLIN R. S. Recovery of antibody combining activity by interaction of different peptide chains isolated from purified horse antitoxins. Folia Microbiol (Praha) 1963 Mar;8:128–130. doi: 10.1007/BF02877236. [DOI] [PubMed] [Google Scholar]
  10. FRANKLIN E. C. STRUCTURAL STUDIES OF HUMAN 7S GAMMA-GLOBULIN (G IMMUNOGLOBULIN). FURTHER OBSERVATIONS OF A NATURALLY OCCURRING PROTEIN RELATED TO THE CRYSTALLIZABLE (FAST) FRAGMENT. J Exp Med. 1964 Nov 1;120:691–709. doi: 10.1084/jem.120.5.691. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. GREY H. M., KUNKEL H. G. H CHAIN SUBGROUPS OF MYELOMA PROTEINS AND NORMAL 7S GAMMA-GLOBULIN. J Exp Med. 1964 Aug 1;120:253–266. doi: 10.1084/jem.120.2.253. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. KORNGOLD L. Antigenic specificity of gamma2-myeloma globulins. J Natl Cancer Inst. 1963 Mar;30:553–567. [PubMed] [Google Scholar]
  13. KUNKEL H. G. Zone electrophoresis. Methods Biochem Anal. 1954;1:141–170. doi: 10.1002/9780470110171.ch6. [DOI] [PubMed] [Google Scholar]
  14. Kunkel H. G., Mannik M., Williams R. C. Individual Antigenic Specificity of Isolated Antibodies. Science. 1963 Jun 14;140(3572):1218–1219. doi: 10.1126/science.140.3572.1218. [DOI] [PubMed] [Google Scholar]
  15. MELTZER M., FRANKLIN E. C., FUNDENBERG H., FRANGIONE B. SINGLE PEPTIDE DIFFERENCES BETWEEN GAMMA-GLOBULINS OF DIFFERENT GENETIC (GM) TYPES. Proc Natl Acad Sci U S A. 1964 Jun;51:1007–1014. doi: 10.1073/pnas.51.6.1007. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. METZGER H., SINGER S. J. BINDING CAPACITY OF REDUCTIVELY FRAGMENTED ANTIBODIES TO THE 2,4-DINITROPHENYL GROUP. Science. 1963 Nov 8;142(3593):674–675. doi: 10.1126/science.142.3593.674. [DOI] [PubMed] [Google Scholar]
  17. 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]
  18. NISONOFF A., WISSLER F. C., LIPMAN L. N. Properties of the major component of a peptic digest of rabbit antibody. Science. 1960 Dec 9;132(3441):1770–1771. doi: 10.1126/science.132.3441.1770. [DOI] [PubMed] [Google Scholar]
  19. OSSERMAN E. F., TAKATSUKI K. CLINICAL AND IMMUNOCHEMICAL STUDIES OF FOUR CASES OF HEAVY (H-GAMMA-2) CHAIN DISEASE. Am J Med. 1964 Sep;37:351–373. doi: 10.1016/0002-9343(64)90192-5. [DOI] [PubMed] [Google Scholar]
  20. 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]
  21. PUTNAM F. W., EASLEY C. W., HELLING J. W. STRUCTURAL STUDY OF HUMAN GAMMA-GLOBULIN THROUGH THE ANALYSIS OF THE TRYPTIC PEPTIDES OF BENCE-JONES PROTEINS. Biochim Biophys Acta. 1963 Oct 8;78:231–233. doi: 10.1016/0006-3002(63)91632-9. [DOI] [PubMed] [Google Scholar]
  22. ROHOLT O. A., RADZIMSKI G., PRESSMAN D. Antibody combining site: the B polypeptide chain. Science. 1963 Aug 23;141(3582):726–727. doi: 10.1126/science.141.3582.726. [DOI] [PubMed] [Google Scholar]
  23. TAKATSUKI K., OSSERMAN E. F. STRUCTURAL DIFFERENCES BETWEEN 2 TYPES OF "HEAVY CHAIN" DISEASE PROTEINS AND MYELOMA GLOBULINS OF CORRESPONDING TYPES. Science. 1964 Jul 31;145(3631):499–500. doi: 10.1126/science.145.3631.499. [DOI] [PubMed] [Google Scholar]
  24. TERRY W. D., FAHEY J. L. SUBCLASSES OF HUMAN GAMMA-2-GLOBULIN BASED ON DIFFERENCES IN THE HEAVY POLYPEPTIDE CHAINS. Science. 1964 Oct 16;146(3642):400–401. doi: 10.1126/science.146.3642.400. [DOI] [PubMed] [Google Scholar]
  25. TODD C. W. Allotypy in rabbit 19S protein. Biochem Biophys Res Commun. 1963 May 3;11:170–175. doi: 10.1016/0006-291x(63)90329-2. [DOI] [PubMed] [Google Scholar]
  26. UTSUMI S., KARUSH F. THE SUBUNITS OF PURIFIED RABBIT ANTIBODY. Biochemistry. 1964 Sep;3:1329–1338. doi: 10.1021/bi00897a024. [DOI] [PubMed] [Google Scholar]

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