Nakagawa H, Debuchi H
Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University, Japan.
Biochem Pharmacol. 1992 Nov 3;44(9):1773-7. doi: 10.1016/0006-2952(92)90071-p.
An active gelatinase has been purified from the conditioned medium of granulation tissue culture formed by carrageenin injection in rats. The purified gelatinase gave a single band corresponding to a M(r) of 57 kDa on both sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and SDS-gelatin PAGE. The granulation tissue-derived gelatinase selectively cleaved the Gln6-Phe7 bond of substance P (SP) with a Km of 0.17 mM and a Vmax of 0.027 nmol SP7-11/min/micrograms protein, resulting in the generation of biologically inactive fragments, SP1-6 and SP7-11. Our data suggest that the gelatinase produced by granulation tissue participates in the inactivation of SP in the inflammatory site.
已从角叉菜胶注射诱导大鼠形成的肉芽组织培养条件培养基中纯化出一种活性明胶酶。纯化后的明胶酶在十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳（SDS - PAGE）和SDS - 明胶PAGE上均呈现出一条对应于57 kDa相对分子质量（M(r)）的条带。肉芽组织来源的明胶酶选择性切割P物质（SP）的Gln6 - Phe7键，其米氏常数（Km）为0.17 mM，最大反应速度（Vmax）为0.027 nmol SP7 - 11/分钟/微克蛋白质，从而产生无生物活性的片段SP1 - 6和SP7 - 11。我们的数据表明，肉芽组织产生的明胶酶参与炎症部位SP的失活过程。
