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. 1970 Nov;7(5):627–640.

Pepsin digestion of human G-myeloma proteins of different subclasses. II. Immunochemical investigations of the products of peptic digestion

M W Turner, H H Bennich, J B Natvig
PMCID: PMC1712887  PMID: 4992782

Abstract

Immunochemical comparisons have been made of the F(ab')2 and the pFc' fragments of each of the four subclasses of human IgG. The F(ab')2 fragments of IgG 3 proteins were found to exhibit anomalous gel-filtration behaviour compared with similar fragments from the other subclasses. This difference was unrelated to carbohydrate content and may indicate a unique conformation for IgG 3 molecules.

The pFc' fragments of all four subclasses were similar in size and antigenically indistinguishable by gel-diffusion tests but on both starch gel electrophoresis and immunoelectrophoresis the IgG 4 pFc' fragment was of faster mobility.

Some minor products of pepsin digestion arising from the IgG 2, IgG 3 and IgG 4 subclasses were also investigated. These fragments were derived from the Fab regions of the respective parent molecules.

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Selected References

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

  1. Abel C. A., Spiegelberg H. L., Grey H. M. The carbohydrate contents of fragments and polypeptide chains of human gamma-G-myeloma proteins of different heavy-chain subclasses. Biochemistry. 1968 Apr;7(4):1271–1278. doi: 10.1021/bi00844a004. [DOI] [PubMed] [Google Scholar]
  2. Andrews P. Estimation of the molecular weights of proteins by Sephadex gel-filtration. Biochem J. 1964 May;91(2):222–233. doi: 10.1042/bj0910222. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. 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]
  4. Dorrington K. J., Rockey J. H. Differences in the molecular size of the heavy chains from gamma A1- and gamma A2-globulins. Biochim Biophys Acta. 1970 Mar 31;200(3):584–586. doi: 10.1016/0005-2795(70)90119-4. [DOI] [PubMed] [Google Scholar]
  5. Frangione B., Milstein C. Partial deletion in the heavy chain disease protein ZUC. Nature. 1969 Nov 8;224(5219):597–599. doi: 10.1038/224597a0. [DOI] [PubMed] [Google Scholar]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. Jerry L. M., Kunkel H. G., Grey H. M. Absence of disulfide bonds linking the heavy and light chains: a property of a genetic variant of gamma-A2 globulins. Proc Natl Acad Sci U S A. 1970 Mar;65(3):557–563. doi: 10.1073/pnas.65.3.557. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Natvig J. B. Human anti-gamma-globulin antibodies specific for gamma G heavy chain subclasses. Immunology. 1970 Jul;19(1):125–135. [PMC free article] [PubMed] [Google Scholar]
  12. Natvig J. B., Kunkel H. G., Joslin F. G. Delineation of two antigenic markers, "non a" and "non g" related to the genetic antigens of human gamma globulin. J Immunol. 1969 Mar;102(3):611–617. [PubMed] [Google Scholar]
  13. OUCHTERLONY O. Diffusion-in-gel methods for immunological analysis. Prog Allergy. 1958;5:1–78. [PubMed] [Google Scholar]
  14. Prahl J. W. Enzymic degradation of the Fc fragment of rabbit immunoglobulin IgG. Biochem J. 1967 Aug;104(2):647–655. doi: 10.1042/bj1040647. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. SVENNERHOLM L. The quantitative estimation of cerebrosides in nervous tissue. J Neurochem. 1956 May;1(1):42–53. doi: 10.1111/j.1471-4159.1956.tb12053.x. [DOI] [PubMed] [Google Scholar]
  16. Smyth D. S., Utsumi S. Structure at the hinge region in rabbit immunoglobulin-G. Nature. 1967 Oct 28;216(5113):332–335. doi: 10.1038/216332a0. [DOI] [PubMed] [Google Scholar]
  17. Turner M. W., Bennich H. H., Natvig J. B. Pepsin digestion of human G-myeloma proteins of different subclasses. I. The characteristic features of pepsin cleavage as a function of time. Clin Exp Immunol. 1970 Nov;7(5):603–625. [PMC free article] [PubMed] [Google Scholar]
  18. 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]
  19. 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]
  20. 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]
  21. Turner M. W., Rowe D. S. Antibodies of IgA and IgG class in normal human urine. Immunology. 1967 Jun;12(6):689–699. [PMC free article] [PubMed] [Google Scholar]
  22. Utsumi S. Stepwise cleavage of rabbit immunoglobulin G by papain and isolation of four types of biologically active Fc fragments. Biochem J. 1969 Apr;112(3):343–355. doi: 10.1042/bj1120343. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. WARREN L. The thiobarbituric acid assay of sialic acids. J Biol Chem. 1959 Aug;234(8):1971–1975. [PubMed] [Google Scholar]

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