Isolation and structure of a cross-linked tripeptide from calf bone collagen.

Abstract:

:A cross-linked tripeptide has been isolated from alkaline hydrolysates of NaB3H4-reduced calf bone collagen. The peptide contains dihydroxylysinonorleucine, the most abundant cross-link in bone collagen, and it has a single N-terminal proline and a single C-terminal valine. These amino acids are in peptide linkage with the cross-link, in a trans configuration with respect to the secondary amine.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Fujii K,Corcoran D,Tanzer ML

doi

10.1021/bi00691a011

subject

Has Abstract

pub_date

1975-10-07 00:00:00

pages

4409-13

issue

20

eissn

0006-2960

issn

1520-4995

journal_volume

14

pub_type

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