Isolation and structure of a cross-linked tripeptide from calf bone collagen.
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.
D000818:Animals; D001665:Binding Sites; D001842:Bone and Bones / Q000032:analysis*; D002417:Cattle; D003094:Collagen / Q000032:analysis; D006901:Hydroxylysine / Q000031:analogs & derivatives / Q000032:analysis; D009646:Norleucine / Q000032:analysis; D009842:Oligopeptides / Q000032:analysis; D011392:Proline / Q000032:analysis; D011485:Protein Binding; D011487:Protein Conformation; D013977:Tibia / Q000032:analysis; D014633:Valine / Q000032:analysis
D009842:Oligopeptides; D006901:Hydroxylysine; D009646:Norleucine; D003094:Collagen; D011392:Proline; D014633:Valine