The chemistry of the collagen cross-links. The absence of reduction of dehydrolysinonorleucine and dehydrohydroxylysinonorleucine in vivo.
Two aldimine bonds have been shown to be present as stabilizing cross-links in intact collagen fibres from soft tissues: dehydrohydroxylysinonorleucine as a major component and dehydrolysinonorleucine being present in trace quantities. In the highly insoluble collagens less dehydrohydroxylysinonorleucine is present but the proportion of dehydrolysinonorleucine increases. In elastin the latter aldimine is reduced in vivo to give a more stable cross-link but no comparable reduction could be detected with either of the aldimines present in collagen.
D000596:Amino Acids / Q000378:metabolism; D000818:Animals; D002356:Cartilage / Q000378:metabolism; D002417:Cattle; D003094:Collagen / Q000032:analysis / Q000378:metabolism*; D003238:Connective Tissue / Q000378:metabolism; D003998:Dicarboxylic Acids / Q000378:metabolism*; D004549:Elastin / Q000378:metabolism; D007097:Imines; D007403:Intervertebral Disc / Q000378:metabolism; D046911:Macromolecular Substances; D010084:Oxidation-Reduction; D014316:Tritium
D000596:Amino Acids; D003998:Dicarboxylic Acids; D007097:Imines; D046911:Macromolecular Substances; D014316:Tritium; D003094:Collagen; D004549:Elastin