Abstract
A component, termed pyridinoline, has been reported to be derived from 'lysine aldehyde' (2,6-diaminohexanaldehyde) and designated as the stable cross-link of mature collagen. Commerically prepared collagen and freshly obtained mature bovine tendon collagen were both investigated with regard to their pyridinoline content. Both sources of material could be depleted of this component by mild washing procedures. Pepsin-solubilized collagen and peptides derived from CNBr cleavage of intact collagen did not contain the compound. Pure pyridinoline was isolated and shown to be hydrolysed by water, as previously reported, but neither hydroxylysine nor lysine could be ds not a cross-linking component of collagen.
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