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. 1964 Feb 29;119(3):443–452. doi: 10.1084/jem.119.3.443

STUDIES ON HUMAN ANTIBODIES

I. STARCH GEL ELECTROPHORESIS OF THE DISSOCIATED POLYPEPTIDE CHAINS

G M Edelman 1, Elvin A Kabat 1
PMCID: PMC2137884  PMID: 14129715

Abstract

Specific precipitates and purified human antibodies were reduced and alkylated and subjected to starch gel electrophoresis in 8 M urea to dissociate and separate the L and H polypeptide chains. Dissociated antibodies to dextran, levan, teichoic acid, blood group A substance, and tetanus toxoid showed sharp bands corresponding to L polypeptide chains. The patterns differed for antibodies of different specificities. Some differences were also seen among antibodies of the same specificity from different individuals. Purified antidextran antibodies showed particularly simple patterns resembling those of purified human γ myeloma proteins. In some cases only one L chain band was present.

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Selected References

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

  1. ALLEN P. Z., KABAT E. A. Persistence of circulating antibodies in human subjects immunized with dextran, levan and blood group substances. J Immunol. 1958 Jun;80(6):495–500. [PubMed] [Google Scholar]
  2. CARBONARA A. O., HEREMANS J. F. Subunits of normal and pathological gama-1A-globulins. (beta-2A-globulins). Arch Biochem Biophys. 1963 Jul;102:137–143. doi: 10.1016/0003-9861(63)90331-x. [DOI] [PubMed] [Google Scholar]
  3. 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]
  4. EDELMAN G. M., BENACERRAF B., OVARY Z. STRUCTURE AND SPECIFICITY OF GUINEA PIG 7S ANTIBODIES. J Exp Med. 1963 Aug 1;118:229–244. doi: 10.1084/jem.118.2.229. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. EDELMAN G. M., BENACERRAF B. On structural and functional relations between antibodies and proteins of the gamma-system. Proc Natl Acad Sci U S A. 1962 Jun 15;48:1035–1042. doi: 10.1073/pnas.48.6.1035. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. EDELMAN G. M., GALLY J. A. The nature of Bence-Jones proteins. Chemical similarities to polypetide chains of myeloma globulins and normal gamma-globulins. J Exp Med. 1962 Aug 1;116:207–227. doi: 10.1084/jem.116.2.207. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
  12. KABAT E. A., BERG D. Dextran; an antigen in man. J Immunol. 1953 Jun;70(6):514–532. [PubMed] [Google Scholar]
  13. KABAT E. A., BEZER A. E. The effect of variation in molecular weight on the antigenicity of dextran in man. Arch Biochem Biophys. 1958 Dec;78(2):306–318. doi: 10.1016/0003-9861(58)90354-0. [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. MERRYMAN C., BENACERRAF B. STUDIES ON THE STRUCTURE OF MOUSE ANTIBODIES. Proc Soc Exp Biol Med. 1963 Nov;114:372–376. doi: 10.3181/00379727-114-28681. [DOI] [PubMed] [Google Scholar]
  16. MORSE S. I. Studies on the chemistry and immunochemistry of cell walls of Staphylococcus aureus. J Exp Med. 1962 Aug 1;116:229–245. doi: 10.1084/jem.116.2.229. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. PUTNAM F. W. Aberrations of protein metabolism in multiple myeloma; interrelationships of abnormal serum globulins and Bence-Jones proteins. Physiol Rev. 1957 Oct;37(4):512–538. doi: 10.1152/physrev.1957.37.4.512. [DOI] [PubMed] [Google Scholar]
  18. 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]
  19. SCHLOSSMAN S. F., KABAT E. A. Specific fractionation of a population of antidextran molecules with combining sites of various sizes. J Exp Med. 1962 Oct 1;116:535–552. doi: 10.1084/jem.116.4.535. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. SLATER R. J., WARD S. M., KUNKEL H. G. Immunological relationships among the myeloma proteins. J Exp Med. 1955 Jan 1;101(1):85–108. doi: 10.1084/jem.101.1.85. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. STROMINGER J. L. Biosynthesis of bacterial cell walls. Fed Proc. 1962 Jan-Feb;21:134–143. [PubMed] [Google Scholar]

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