An investigation of pyridinoline, a putative collagen cross-link

Author:

Elsden D F,Light N D,Bailey A J

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.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

Cited by 24 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

1. Analysis of the Crosslinking Components in Collagen and Elastin;Methods of Biochemical Analysis;2006-10-31

2. Collagen cross-links: location of pyridinoline in type I collagen;FEBS Letters;1985-03-25

3. Ultraviolet light- and ozone-induced changes in pyridinoline, a trisubstituted 3-hydroxypyridinium crosslink of collagen;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1985-03

4. Blue autofluorescence of human achilles tendon collagen in relation to aging.;ACTA HISTOCHEMICA ET CYTOCHEMICA;1985

5. The Protein Amino Acids;Chemistry and Biochemistry of the Amino Acids;1985

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