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  • Title: Cartilage type IX collagen is cross-linked by hydroxypyridinium residues.
    Author: Wu JJ, Eyre DR.
    Journal: Biochem Biophys Res Commun; 1984 Sep 28; 123(3):1033-9. PubMed ID: 6487319.
    Abstract:
    Type IX collagen, a recently discovered, unusual protein of cartilage, has a segmented triple-helical structure containing interchain disulfides. Its polymeric form and function are unknown. When prepared by pepsin from bovine articular cartilage, type IX collagen was found to contain a high concentration of hydroxypyridinium cross-links, similar to that in type II collagen. Fluorescence spectroscopy located the hydroxylysyl pyridinoline and lysyl pyridinoline cross-linking residues exclusively in the high-molecular-weight collagen fraction, from which they were recovered predominantly in a single CNBr-derived peptide. The results point to a structural role for type IX collagen in cartilage matrix, possibly as an adhesion material to type II collagen fibrils.
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