Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1965 Mar;94(3):742–750. doi: 10.1042/bj0940742

Characterization of lamprey fibrinopeptides

R F Doolittle 1,*
PMCID: PMC1206610  PMID: 14340066

Abstract

1. Lamprey fibrinopeptide B is a relatively large peptide made up of about 40 amino acid residues. The peptide is highly electronegative, containing a large number of aspartic acid residues and a tyrosine O-sulphate residue. 2. The amino acid sequence of the first 18 residues from the N-terminal end of fibrinopeptide B has been established. The C-terminal ends with the sequence Val-Arg. Fibrino-peptide B is released by both lamprey and bovine thrombins. 3. Lamprey fibrino-peptide A is a short peptide containing only eight residues. The proposed amino acid sequence is: Asp-Asp-Ser-Ile/Leu-Asp-Ser-Leu/Ile-ArgThis peptide is released by lamprey thrombin but not by bovine thrombin.

Full text

PDF
742

Selected References

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

  1. ACHER R., CROCKER C. Réactions colorées spécifiques de l'arginine et de la tyrosine réalisées après chromatographie sur papier. Biochim Biophys Acta. 1952 Dec;9(6):704–705. doi: 10.1016/0006-3002(52)90236-9. [DOI] [PubMed] [Google Scholar]
  2. BLACKBURN S., LEE G. R. The liberation of aspartic acid during the acid hydrolysis of proteins. Biochem J. 1954 Oct;58(2):227–231. doi: 10.1042/bj0580227. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. BLOMBACK B., BOSTROM H., VESTERMARK A. On the [35S]sulphate incorporation in fibrinopeptide B from rabbit fibrinogen. Biochim Biophys Acta. 1960 Mar 11;38:502–512. doi: 10.1016/0006-3002(60)91285-3. [DOI] [PubMed] [Google Scholar]
  4. BREITENBACH J. W., DERKOSCH J., WESSELY F. Energetics of peptide formation. Nature. 1952 May 31;169(4309):922–922. doi: 10.1038/169922a0. [DOI] [PubMed] [Google Scholar]
  5. DOOLITTLE R. F., BLOMBAECK B. AMINO-ACID SEQUENCE INVESTIGATIONS OF FIBRINOPEPTIDES FROM VARIOUS MAMMALS: EVOLUTIONARY IMPLICATIONS. Nature. 1964 Apr 11;202:147–152. doi: 10.1038/202147a0. [DOI] [PubMed] [Google Scholar]
  6. DOOLITTLE R. F. DIFFERENCES IN THE CLOTTING OF LAMPREY FIBRINOGEN BY LAMPREY AND BOVINE THROMBINS. Biochem J. 1965 Mar;94:735–741. doi: 10.1042/bj0940735. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. EDMAN P. Phenylthiohydantoins in protein analysis. Ann N Y Acad Sci. 1960 Aug 31;88:602–610. doi: 10.1111/j.1749-6632.1960.tb20056.x. [DOI] [PubMed] [Google Scholar]
  8. HIRS C. H., MOORE S., STEIN W. H. Peptides obtained by tryptic hydrolysis of performic acid-oxidized ribonuclease. J Biol Chem. 1956 Apr;219(2):623–642. [PubMed] [Google Scholar]
  9. MOORE S., STEIN W. H. A modified ninhydrin reagent for the photometric determination of amino acids and related compounds. J Biol Chem. 1954 Dec;211(2):907–913. [PubMed] [Google Scholar]
  10. MOORE S., STEIN W. H. Procedures for the chromatographic determination of amino acids on four per cent cross-linked sulfonated polystyrene resins. J Biol Chem. 1954 Dec;211(2):893–906. [PubMed] [Google Scholar]
  11. McMENAMY R. H., LUND C. C., ONCLEY J. L. Unbound amino acid concentrations in human blood plasmas. J Clin Invest. 1957 Dec;36(12):1672–1679. doi: 10.1172/JCI103568. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. REDDI K. K., KODICEK E. Metabolism of nicotinic acid and related compounds in man and rat. Biochem J. 1953 Jan;53(2):286–294. doi: 10.1042/bj0530286. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES