Collagen type IX: Evidence for covalent linkages to type II collagen in cartilage |
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Authors: | David R. Eyre Stephen Apon Jiann-Jiu Wu Lowell H. Ericsson Kenneth A. Walsh |
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Affiliation: | 1. Departments of Orthopaedics, University of Washington, Seattle, WA 98195, USA;2. Departments of Biochemistry, University of Washington, Seattle, WA 98195, USA |
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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. |
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Keywords: | Collagen Cross-linking Amino acid sequence (Bovine cartilage) |
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