The chemistry of the collagen cross-links. The mechanism of stabilization of the reducible intermediate cross-links
- 1 August 1975
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 149 (2) , 381-385
- https://doi.org/10.1042/bj1490381
Abstract
The periodate-degradation technique was used to demonstrate the mechanism by which the reducible cross-links of collagen are stabilized. In all the tissues examined, Smith degradations of the 3H-labelled cross-links indicated that dihydroxylysinonorleucine is derived solely from hydroxylysino-5-oxonorleucine, the Amadori-rearranged product of the original condensation reaction. Monohydroxylysinonorleucine exists in both keto and aldimine forms, the former being derived from hydroxyallysine and the latter from allysine. Their relative proportions are tissue-dependent and are related to the degree of hydroxylation of the specific lysine residues in both the telopeptides and the triple helix.Keywords
This publication has 21 references indexed in Scilit:
- Age-related variations in hydroxylation of lysine and proline in collagenBiochemical Journal, 1974
- Stable crosslinks of collagenBiochemical and Biophysical Research Communications, 1973
- Isolation of polypeptides containing the intermolecular cross-link δ,δ′-dihydroxylysinonorleucine from dentin collagenArchives of Biochemistry and Biophysics, 1973
- Isolation and characterization of the cyanogen bromide peptides from the αl(II) chain of bovine and human cartilage collagenBiochemistry, 1973
- Relative stabilities of the intermediate reducible crosslinks present in collagen fibresFEBS Letters, 1973
- The chemistry of the collagen cross-links. Age-related changes in the reducible components of intact bovine collagen fibresBiochemical Journal, 1973
- Studies on the location of intermolecular crosslinks in collagen. Isolation of a cyanogen bromide peptide containing δ-hydroxylysinonorleucineBiochemistry, 1972
- Hydroxylysine in the N-terminal regions of the α1- and α2-chains of various collagensBiochemical Journal, 1971
- Collagen cross-linking: Identification of two cyanogen bromide peptides containing sites of intermolecular cross-link formation in cartilage collagenBiochemical and Biophysical Research Communications, 1971
- Isolation and characterization of the peptides derived from the α1 chain of chick bone collagen after cyanogen bromide cleavageBiochemistry, 1969