Enzymic degradation of the Fc fragment of rabbit immunoglobulin IgG - PubMed (original) (raw)
Enzymic degradation of the Fc fragment of rabbit immunoglobulin IgG
J W Prahl. Biochem J. 1967 Aug.
Abstract
The digestion of the Fc fragment of rabbit immunoglobulin IgG by several proteolytic enzymes was investigated by using gel filtration and starch-gel electrophoresis in 8m-urea-formate as criteria of the extent of degradation. Though fragment Fc and mildly reduced fragment Fc proved resistant to tryptic hydrolysis, papain and pepsin cleaved the fragment at acidic pH values and appeared to give rise to a similar spectrum of products. A (limit) peptide comprising the C-terminal 113 residues of the heavy chain was isolated and identified from the pepsin-digest products of fragment Fc. The products of proteolytic digestion of fragment Fc were no longer able to inhibit passive cutaneous anaphylaxis by rabbit anti-(bovine serum albumin) or demonstrate reversed passive cutaneous anaphylaxis in the guinea pig. Nor were they able to inhibit the intestinal absorption of heterologous immunoglobulin IgG in the young mouse. These studies imply that the site or sites responsible for these biological properties of intact fragment Fc reside in the N-terminal 30-40% of the fragment.
Similar articles
- Stepwise cleavage of rabbit immunoglobulin G by papain and isolation of four types of biologically active Fc fragments.
Utsumi S. Utsumi S. Biochem J. 1969 Apr;112(3):343-55. doi: 10.1042/bj1120343. Biochem J. 1969. PMID: 4979349 Free PMC article. - The products from papain and pepsin hydrolyses of guinea-pig immunoglobulins gamma 1G and gamma 2 G.
Leslie RG, Melamed MD, Cohen S. Leslie RG, et al. Biochem J. 1971 Mar;121(5):829-37. doi: 10.1042/bj1210829. Biochem J. 1971. PMID: 4107091 Free PMC article. - Subfragments from the Fc fragment of human immunoglobulin G. Isolation and physicochemical charaterization.
Turner MW, Bennich H. Turner MW, et al. Biochem J. 1968 Mar;107(2):171-8. doi: 10.1042/bj1070171. Biochem J. 1968. PMID: 4171016 Free PMC article. - Physiochemical characterization of proteolytic cleavage fragments of bovine colostral immunoglobulin G1 (IgG1).
Fang WD, Mukkur TK. Fang WD, et al. Biochem J. 1976 Apr 1;155(1):25-30. doi: 10.1042/bj1550025. Biochem J. 1976. PMID: 779768 Free PMC article.
Cited by
- Conformation changes and dissociation of Fc fragments of rabbit immunoglobulin G as a function of pH.
Charlwood PA, Utsumi S. Charlwood PA, et al. Biochem J. 1969 Apr;112(3):357-65. doi: 10.1042/bj1120357. Biochem J. 1969. PMID: 5801306 Free PMC article. - Independent folding of the variable and constant halves of a lambda immunoglobulin light chain.
Björk I, Karlsson FA, Berggård I. Björk I, et al. Proc Natl Acad Sci U S A. 1971 Aug;68(8):1707-10. doi: 10.1073/pnas.68.8.1707. Proc Natl Acad Sci U S A. 1971. PMID: 5288755 Free PMC article. - Pepsin digestion of human G-myeloma proteins of different subclasses. II. Immunochemical investigations of the products of peptic digestion.
Turner MW, Bennich HH, Natvig JB. Turner MW, et al. Clin Exp Immunol. 1970 Nov;7(5):627-40. Clin Exp Immunol. 1970. PMID: 4992782 Free PMC article. - Stepwise cleavage of rabbit immunoglobulin G by papain and isolation of four types of biologically active Fc fragments.
Utsumi S. Utsumi S. Biochem J. 1969 Apr;112(3):343-55. doi: 10.1042/bj1120343. Biochem J. 1969. PMID: 4979349 Free PMC article. - Intrachain disulphide bridges in immunoglobulin G heavy chains. The Fc fragment.
Frangione B, Milstein C, Franklin EC. Frangione B, et al. Biochem J. 1968 Jan;106(1):15-21. doi: 10.1042/bj1060015. Biochem J. 1968. PMID: 4889360 Free PMC article.
References
- J Biol Chem. 1962 Aug;237:2547-61 - PubMed
- Proc R Soc Lond B Biol Sci. 1966 Nov 22;166(1003):159-75 - PubMed
- Biochem J. 1955 Mar;59(3):405-10 - PubMed
- Arch Biochem Biophys. 1962 Sep;Suppl 1:174-80 - PubMed
- Proc R Soc Lond B Biol Sci. 1960 Mar 1;151:478-82 - PubMed
MeSH terms
Substances
LinkOut - more resources
Full Text Sources