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Science 11 May 1973:
Vol. 180. no. 4086, pp. 561 - 566
DOI: 10.1126/science.180.4086.561
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Articles

Cross-Linking of Collagen

Marvin L. Tanzer 1

1 The Department of Biochemistry, University of Connecticut Health Center, Farmnington 06032.

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.


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