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.