Isolation and Characterization of the Cyanogen Bromide Peptides from the αl and α2 Chains of Acid-Soluble Bovine Skin Collagen

Dino Volpin, Arthur Veis

Research output: Contribution to journalArticle

42 Scopus citations

Abstract

The al and al chains of acid-soluble steer skin collagen were cleaved with CNBr and the resulting fragments were separated by ion-exchange chromatography. The sum of the amino acids of the eight peptides isolated from al are in good agreement with the amino acid composition of the αl chain. The six peptides isolated from the CNBr digested α2 chain also accounted for the amino acid content of α2. In each case, the peptides are similar and clearly homologous to the cyanogen bromide peptides previously isolated from rat skin, human skin, chicken skin, and bone collagens. However, the short, nonhelical, NH2-terminal end of the al chain is Variable in that it may lack a NH2-terminal tetrapeptide (Glu, Leu, Ser, Tyr). The dipeptide αl-CBO, present in chicken and in rat tendon, but absent in human skin collagen, is not present in bovine skin collagen.

Original languageEnglish (US)
Pages (from-to)1751-1755
Number of pages5
JournalBiochemistry
Volume10
Issue number10
DOIs
StatePublished - May 1 1971

ASJC Scopus subject areas

  • Biochemistry

Fingerprint Dive into the research topics of 'Isolation and Characterization of the Cyanogen Bromide Peptides from the αl and α2 Chains of Acid-Soluble Bovine Skin Collagen'. Together they form a unique fingerprint.

  • Cite this