Home LiteratureArticle Details
PMID: 13982985 Published · ppublish English Journal Article

Tropocollagen: significance of protease-induced alterations.

Science (New York, N.Y.) ·Vol. 139 ·No. 3549 ·1963-01-04 ·Pages 37-9

RUBIN AL, PFAHL D, SPEAKMAN PT, DAVISON PF, SCHMITT FO

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
MeSH Terms
Amino Acids Collagen Macromolecular Substances Pepsin A Peptide Hydrolases Peptides Tropocollagen
Chemicals
Amino Acids Macromolecular Substances Peptides Tropocollagen Collagen Peptide Hydrolases Pepsin A
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
RUBIN A L
PFAHL D
SPEAKMAN P T
DAVISON P F
SCHMITT F O
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1963-01-04
Pages
37-9
Language
English
Region
United States
NLM ID
0404511
Subset
OM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com