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J. Biochem, 1978, Vol. 83, No. 3 863-867
© 1978 Japanese Biochemical Society

research-article

Pyridinoline, a Non-Reducible Crosslink of Collagen

Quantitative Determination, Distribution, and Isolation of a Crosslinked Peptide.

Daisaburo FUJIMOTO* and Takahiko MORIGUCHI**

*Department of Chemistry Hamamatsu University School of Medicine Hamamatsu, Shizuoka 431–31
**Department of Dermatology, Hamamatsu University School of Medicine Hamamatsu, Shizuoka 431–31

Pyridinoline is a crosslink compound isolated from bovine Achilles tendon collagen. It is a 3-hydroxypyridinium derivative with three amino and three carboxyl groups (Fujimoto, D., Akiba, K., & Nakamura, N. (1977) Biochem. Biophys. Res. Commun. 76, 1124–1129). The contents of pyridinoline in collagens from various sources were determined. The pyridinoline content of bovine Achilles tendon was 0.16 residue per 1,000 residues and that of rat Achilles tendon collagen was 0.017 residue per 1,000 residues. Besides Achilles tendon collagens, pyridinoline was found in collagens from coastal cartilage, rib and femoral bone of rat. It was not found in collagens from the tail tendon and skin of rat. A crosslinked, triple-chained peptide containing pyridinoline was isolated from bovine Achilles tendon collagen after digestion with pronase. Its amino acid composition suggests that the peptide may be involved in an intermolecular crosslink among a carboxyterminal sequence, a sequence near the aminoterminus and a sequence in the helical region.


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