Skip to main content
NCBI home page
Clinical and Experimental Immunology logoLink to Clinical and Experimental Immunology
. 1970 Nov;7(5):603–625.

Pepsin digestion of human G-myeloma proteins of different subclasses. I. The characteristic features of pepsin cleavage as a function of time

M W Turner, H H Bennich, J B Natvig
PMCID: PMC1712889  PMID: 4924105

Abstract

The techniques of starch gel electrophoresis, immunoelectrophoresis and high resolution gel filtration have been used to investigate the peptic cleavage of human G-myeloma proteins of the four known subclasses. The appearance and fate of F(ab')2 and pFc' fragments and the persistence of undegraded IgG have been contrasted and distinctive patterns of pepsin sensitivity have been established for each subclass. The IgG 1 subclass is the most resistant and is degraded by pepsin in a manner which is closely similar to that observed for pooled IgG. IgG 2 molecules are also relatively resistant to peptic cleavage whereas IgG 3 and IgG 4 proteins are much more sensitive. Nevertheless all the subclasses are cleaved by the enzyme in similar susceptible regions and give rise at some stage to the same products: F(ab')2 fragment, pFc' fragment and peptides from the N-terminal half of the Fc region.

Full text

PDF
603

Images in this article

608Fig. 1
on p.608
609Fig. 2
on p.609
611Fig. 5
on p.611
612Fig. 6
on p.612
615Fig. 10
on p.615
616Fig. 10
on p.616
617Fig. 11
on p.617
620Fig. 15
on p.620
620Fig. 16
on p.620
622Fig. 19
on p.622

Selected References

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

  1. Bennich H., Turner M. W. The release of Fe' and pFc' fragments from human immunoglobulin G following enzymic digestion: a time study. Biochim Biophys Acta. 1969 Mar;175(2):388–395. doi: 10.1016/0005-2795(69)90016-6. [DOI] [PubMed] [Google Scholar]
  2. 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]
  3. FAHEY J. L., MCLAUGHLIN C. PREPARATION OF ANTISERA SPECIFIC FOR 6.6 S GAMMA-GLOBULINS, BETA 2A-GLOBULINS, GAMMA-1.-MACROGLOBULINS, AND FOR TYPE I AND II COMMON GAMMA-GLOBULIN DETERMINANTS. J Immunol. 1963 Oct;91:484–497. [PubMed] [Google Scholar]
  4. Frangione B., Milstein C., Pink J. R. Structural studies of immunoglobulin G. Nature. 1969 Jan 11;221(5176):145–148. doi: 10.1038/221145a0. [DOI] [PubMed] [Google Scholar]
  5. GRABAR P., WILLIAMS C. A. Méthode permettant l'étude conjuguée des proprietés électrophorétiques et immunochimiques d'un mélange de protéines; application au sérum sanguin. Biochim Biophys Acta. 1953 Jan;10(1):193–194. doi: 10.1016/0006-3002(53)90233-9. [DOI] [PubMed] [Google Scholar]
  6. Gergely J., Fudenberg H. H., van Loghem E. The papain susceptibility of IgG myeloma proteins of different heavy chain subclasses. Immunochemistry. 1970 Jan;7(1):1–6. doi: 10.1016/0019-2791(70)90025-x. [DOI] [PubMed] [Google Scholar]
  7. Heimer R., Schnoll S. S., Primack A. Products of the peptic digestion of human gamma-G-immunoglobulin. Biochemistry. 1967 Jan;6(1):127–134. doi: 10.1021/bi00853a022. [DOI] [PubMed] [Google Scholar]
  8. Jefferis R., Weston P. D., Stanworth D. R., Clamp J. R. Relationship between the papain sensitivity of human gammaG immunoglobulins and their heavy chain subclass. Nature. 1968 Aug 10;219(5154):646–649. doi: 10.1038/219646b0. [DOI] [PubMed] [Google Scholar]
  9. Kunkel H. G., Yount W. J., Litwin S. D. Genetically determined antigen of the Ne subgroup of gamma-globulin: detection by precipitin analysis. Science. 1966 Nov 25;154(3752):1041–1043. doi: 10.1126/science.154.3752.1041. [DOI] [PubMed] [Google Scholar]
  10. Medgyesi G. A., Gergely J. Structural studies of immunoglobulins. 3. Susceptibility of human gamma G globulins to peptic hydrolysis and papain sensitivity of F(ab')2 fragments. Immunochemistry. 1969 May;6(3):473–479. [PubMed] [Google Scholar]
  11. Poulik M. D., Shuster J. Role of cysteine in the production of Fc and F'c sub-components of gamma-G myeloma globulins. Nature. 1965 Sep 4;207(5001):1092–1093. doi: 10.1038/2071092a0. [DOI] [PubMed] [Google Scholar]
  12. Turner M. W., Bennich H. H., Natvig J. B. Pepsin digestion of human G-myeloma proteins of different subclasses. II. Immunochemical investigations of the products of peptic digestion. Clin Exp Immunol. 1970 Nov;7(5):627–640. [PMC free article] [PubMed] [Google Scholar]
  13. Turner M. W., Bennich H. H., Natvig J. B. Simple method of subtyping human G-myeloma proteins based on sensitivity to pepsin digestion. Nature. 1970 Feb 28;225(5235):853–855. doi: 10.1038/225853b0. [DOI] [PubMed] [Google Scholar]
  14. Turner M. W., Bennich H. Subfragments from the Fc fragment of human immunoglobulin G. Isolation and physicochemical charaterization. Biochem J. 1968 Mar;107(2):171–178. doi: 10.1042/bj1070171. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Turner M. W., Natvig J. B., Bennich H. H. Isolation and antigenic characterization of pFc' fragments from six genetically different human G myeloma proteins. FEBS Lett. 1970 Feb 16;6(3):193–197. doi: 10.1016/0014-5793(70)80055-2. [DOI] [PubMed] [Google Scholar]
  16. Williams R. C., Jr, Lawrence T. G., Jr Variations among gamma-globulins at the antigenic site revealed by pepsin digestion. J Clin Invest. 1966 May;45(5):714–723. doi: 10.1172/JCI105386. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Clinical and Experimental Immunology are provided here courtesy of British Society for Immunology

RESOURCES