作者: Henning Birkedal-Hansen
DOI: 10.1016/0076-6879(87)44177-3
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摘要: Publisher Summary This chapter focuses on the catabolism and turnover of collagens. Vertebrate collagenases are endopeptidases capable cleaving helical domain native collagen molecules under physiological conditions. Collagen types I, II, III cleaved, although at different rates, 2 by same "interstitial" or "type I - II collagenase. Scission component a-chains triple helix occurs a single characteristic site, Gly-Ile Gly-Leu bond, located about one-fourth distance from COOH-terminus. Denatured α-chains in random coil configuration also cleaved but much slower rate than triple-helical molecules. discusses detection measurement collagenolytic activity. Although biologic function neither collagenase has yet been established beyond doubt there is considerable substantial evidence to suggest that interstitial involved extracellular dissolution metabolic degradation type and, possibly, presents enzymatic hydrolysis collagen. conclude with competition ELISA human fibroblast