| Literature DB >> 334268 |
D Collins, K Lindberg, B McLees, S Pinnell.
Abstract
A hydroxylysine-rich type I collagen has been isolated from pepsin-digested porcine heart valve. The ratio of alpha1 to alpha2 in the isolated molecule was 2:1. The component alpha chains exhibited unusual chromatographic behavior in comparison to corresponding chains from human dermis and lathyritic rat skin collagen. The composition of component cyanogen bromide peptides identified the alpha chains as authentic type I chains and demonstrated hydroxylysine enrichment throughout the length of the chain. delta6-Dehydro-5,5'dihydroxylysinonorleucine, a collagen cross-link derived from two hydroxylysyl residues and ordinarily found in hard tissue collagens was found to be the predominant cross-link in heart valve.Entities:
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Year: 1977 PMID: 334268 DOI: 10.1016/0005-2795(77)90247-1
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002