弹性蛋白酶
劈理(地质)
化学
多形核白细胞
生物化学
生物
体外
酶
古生物学
断裂(地质)
作者
Carlo L. Mainardi,David L. Hasty,Jerome M. Seyer,A H Kang
标识
DOI:10.1016/s0021-9258(19)70234-8
摘要
Purified polymorphonuclear leukocyte elastase degraded native human liver type I11 collagen at 27OC by making a cleavage through the triple helix.The enzyme had no effect on human type I collagen.The reaction was inhibited by phenylmethanesulfonyl fluoride (PhCHZSOzF) but not by EDTA.The collagen reaction products were identical with those generated by human rheumatoid synovial collagenase when analyzed by polyacrylamide gel electrophoresis and gel filtration.NHAerminal sequence analysis indicated that the enzyme cleaved at an isoleucyl-threonyl bond located 4 residues on the carboxyl side of the established cleavage site for animal collagenases.Therefore, it is likely that in pathologic states, type 111 collagen can be selectively depleted from the matrix by this enzyme.
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