| Literature DB >> 13982985 |
A L RUBIN, D PFAHL, P T SPEAKMAN, P F DAVISON, F O SCHMITT.
Abstract
Interaction properties of tropocollagen are markedly altered by treatment with pepsin. This treatment liberates terminal or near-terminal covalently bonded peptides whose amino acid composition is strikingly different from the composition of the pepsin-resistant triple-helix body of the macromolecule. Pepsin also converts most of the beta-chains to alpha-chains. This fact indicates that the interchain link is also external to the body of the macromolecule and probably involves peptides. The role of these properties in bioregulative mechanisms is briefly discussed.Keywords: COLLAGEN; PEPTIDE HYDROLASES; PEPTIDES
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Year: 1963 PMID: 13982985 DOI: 10.1126/science.139.3549.37
Source DB: PubMed Journal: Science ISSN: 0036-8075 Impact factor: 47.728