Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1977 Jan 1;161(1):185–187. doi: 10.1042/bj1610185

An addition at the C-terminus of water-buffalo immunoglobin lambda chains.

J Svasti
PMCID: PMC1164488  PMID: 403908

Abstract

The amino acid sequence of the C-terminal tryptic peptide of pooled water-buffalo immunoglobulin lambda chains was determined as Thr-Val-Lys-Pro-Ser-Glu-Cys-Pro-Ser. This sequence is closely homologous to equivalent sequences from other species, but shows an additional amino acid on the C-terminal side of the interchain half-cystine residue.

Full text

PDF
185

Selected References

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

  1. Beale D., Squires M. C-terminal amino-acid sequence of bovine immunoglobulin light chain. Nature. 1970 Jun 13;226(5250):1056–1056. doi: 10.1038/2261056a0. [DOI] [PubMed] [Google Scholar]
  2. Brown J. R., Hartley B. S. Location of disulphide bridges by diagonal paper electrophoresis. The disulphide bridges of bovine chymotrypsinogen A. Biochem J. 1966 Oct;101(1):214–228. doi: 10.1042/bj1010214. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. 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]
  4. Grant J. A., Sanders B., Hood L. Partial amino acid sequences of chicken and turkey immunoglobulin light chains. Homology with mammalian lambda chains. Biochemistry. 1971 Aug 3;10(16):3123–3132. doi: 10.1021/bi00792a022. [DOI] [PubMed] [Google Scholar]
  5. Hjertén S., Jerstedt S., Tiselius A. Some aspects of the use of "continuous" and "discontinuous" buffer systems in polyacrylamide gel electrophoresis. Anal Biochem. 1965 May;11(2):219–223. doi: 10.1016/0003-2697(65)90008-4. [DOI] [PubMed] [Google Scholar]
  6. Milstein C. P., Feinstein A. Comparative studies of two types of bovine immunoglobulin G heavy chains. Biochem J. 1968 Apr;107(4):559–564. doi: 10.1042/bj1070559. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Milstein C. The disulphide bridges of immunoglobulin kappa-chains. Biochem J. 1966 Nov;101(2):338–351. doi: 10.1042/bj1010338. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Novotý J., Franek F. N- and C-terminal sequences in pig immunoglobulin pi-chains: Assignment to the K type. FEBS Lett. 1968 Dec;2(2):93–96. doi: 10.1016/0014-5793(68)80111-5. [DOI] [PubMed] [Google Scholar]
  9. PIERCE A. E., FEINSTEIN A. BIOPHYSICAL AND IMMUNOLOGICAL STUDIES ON BOVINE IMMUNE GLOBULINS WITH EVIDENCE FOR SELECTIVE TRANSPORT WITHIN THE MAMMARY GLAND FROM MATERNAL PLASMA TO COLOSTRUM. Immunology. 1965 Jan;8:106–123. [PMC free article] [PubMed] [Google Scholar]
  10. Pink J. R., Buttery S. H., De Vries G. M., Milstein C. Human immunoglobulin subclasses. Partial amino acid sequence of the constant region of a gamma 4 chain. Biochem J. 1970 Mar;117(1):33–47. doi: 10.1042/bj1170033. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Strausbauch P. H., Hurwitz E., Givol D. Interchain disulfide bonds of goat immunoglobulin G. Biochemistry. 1971 Jun 8;10(12):2231–2237. doi: 10.1021/bi00788a008. [DOI] [PubMed] [Google Scholar]
  12. Weber K., Pringle J. R., Osborn M. Measurement of molecular weights by electrophoresis on SDS-acrylamide gel. Methods Enzymol. 1972;26:3–27. doi: 10.1016/s0076-6879(72)26003-7. [DOI] [PubMed] [Google Scholar]

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

RESOURCES