FEBS Lett. 1987 Aug 17;220(2):337-41.

Collagen type IX: evidence for covalent linkages to type II collagen in cartilage.

Eyre DR, Apon S, Wu JJ, Ericsson LH, Walsh KA.

Abstract

A major site of pyridinoline cross-linking in bovine type IX collagen was traced to a tryptic peptide derived from one of the molecule's HMW chains. This peptide gave two amino acid sequences (in 2/1 ratio) consistent with it being a three-chained structure. The major sequence matched exactly that of the C-telopeptide of type II collagen from the same tissue. A second HMW chain that contained pyridinoline cross-links also gave two amino-terminal sequences, one from its own amino terminus, the other matching exactly the N-telopeptide cross-linking sequence of type II collagen. We conclude that type IX collagen molecules are covalently cross-linked in cartilage to molecules of type II collagen, probably at fibril surfaces.

PMID:: 3609327; [PubMed - indexed for MEDLINE]

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Identification of cross-linking sites in bovine cartilage type IX collagen reveals an antiparallel type II-type IX molecular relationship and type IX to type IX bonding. [J Biol Chem. 1992]
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Collagen type IX: evidence for covalent linkages to type II collagen in cartilag...
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Collagen type IX: evidence for covalent linkages to type II collagen in cartilage.

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