Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1970 Jan;116(2):261–268. doi: 10.1042/bj1160261

The disulphide bonds of the heavy chain of rabbit immunoglobulin G

I J O'Donnell 1,*, B Frangione 1,, R R Porter 1
PMCID: PMC1185354  PMID: 5461107

Abstract

Six peptides containing eight half-cystine residues were isolated in good yield, after either oxidation or reduction and carboxymethylation of fragment C-1, which contains the N-terminal half of the heavy chain of rabbit immunoglobulin G. The sequences of five of these peptides had been reported previously (Cebra, Steiner & Porter, 1968b; Wilkinson, 1969) and that of the sixth was established. Other peptides containing half-cystine residues were isolated in much lower yield and are presumed to be derived from minor sequence variants. The cystine-containing peptides from enzymic digests of whole immunoglobulin G and Fc fraction were studied by several techniques and the results obtained enable us to put forward a scheme of the arrangement of the inter- and intra-chain disulphide bonds.

Full text

PDF
261

Selected References

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

  1. Cebra J. J., Givol D., Porter R. R. Common peptides from the N-terminal half of heavy chain of immunoglobulin G from normal rabbit serum and a specific antibody. Biochem J. 1968 Mar;107(1):69–77. doi: 10.1042/bj1070069. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Cebra J. J., Steiner L. A., Porter R. R. The partial sequence of two large peptides from the N-terminal half of heavy chains from normal rabbit immunoglobulin G. Biochem J. 1968 Mar;107(1):79–88. doi: 10.1042/bj1070079. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Consden R., Gordon A. H. A study of the peptides of cystine in partial hydrolysates of wool. Biochem J. 1950 Jan;46(1):8–20. doi: 10.1042/bj0460008. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Frangione B. Correlation of the c-terminal sequence of rabbit light chains with allotypes. FEBS Lett. 1969 Jun;3(5):341–342. doi: 10.1016/0014-5793(69)80173-0. [DOI] [PubMed] [Google Scholar]
  5. Frangione B., Milstein C. Disulphide bridges of immunoglobin G-1 heavy chains. Nature. 1967 Dec 2;216(5118):939–941. doi: 10.1038/216939b0. [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. Frangione B., Milstein C. Variations in the S-S bridges of immunoglobins G: interchain disulfide bridges of gamma G3 myeloma proteins. J Mol Biol. 1968 May 14;33(3):893–906. doi: 10.1016/0022-2836(68)90326-4. [DOI] [PubMed] [Google Scholar]
  8. Fruchter R. G., Jackson S. A., Mole L. E., Porter R. R. Sequence studies of the Fd section of the heavy chain of rabbit immunoglobulin G. Biochem J. 1970 Jan;116(2):249–259. doi: 10.1042/bj1160249. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. PALMER J. L., NISONOFF A. DISSOCIATION OF RABBIT GAMMA-GLOBULIN INTO HALF-MOLECULES AFTER REDUCTION OF ONE LABILE DISULFIDE BOND. Biochemistry. 1964 Jun;3:863–869. doi: 10.1021/bi00894a024. [DOI] [PubMed] [Google Scholar]
  10. Prahl J. W., Porter R. R. Allotype-related sequence variation of the heavy chain of rabbit immunoglobulin G. Biochem J. 1968 May;107(6):753–763. doi: 10.1042/bj1070753. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Press E. M., Piggot P. J., Porter R. R. The N- and c-terminal amino acid sequences of the heavy chain from a pathological human immunoglobulin IgG. Biochem J. 1966 May;99(2):356–366. doi: 10.1042/bj0990356. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Steiner L. A., Porter R. R. The interchain disulfide bonds of a human pathological immunoglobulin. Biochemistry. 1967 Dec;6(12):3957–3970. doi: 10.1021/bi00864a043. [DOI] [PubMed] [Google Scholar]
  13. Wilkinson J. M. Variation in the N-terminal sequence of heavy chains of immunoglobulin G from rabbits of different allotype. Biochem J. 1969 Apr;112(2):173–185. doi: 10.1042/bj1120173. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES