Cross-linking of collagen.

Science (New York, N.Y.) (1973-05-11)
M L Tanzer
ABSTRACT

The formation of collagen cross-links is attributable to the presence of two aldehyde-containing amino acids which react with other amino acids in collagen to generate difunctional, trifunctional, and tetrafunctional cross-links. A necessary prerequisite for the development of these cross-links is that the collagen molecules be assembled in the naturally occurring fibrous polymer. Once this condition is met, cross-linking occurs in a spontaneous, progressive fashion. The chemical structures of the cross-links dictate that very precise intermolecular alignments must occur in the collagen polymer. This seems to be a function of each specific collagen because the relative abundance of the different cross-links varies markedly, depending upon the tissue of origin of the collagen.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Collagen from bovine achilles tendon, powder, suitable for substrate for collagenase