Hatcher V B, Lazarus G S, Levine N, Burk P G, Yost F J
Biochim Biophys Acta. 1977 Jul 8;483(1):160-71. doi: 10.1016/0005-2744(77)90018-3.
A proteinase (EC 3.4.-.-) active at physiological pH has been isolated from human skin utilizing gel filtration and affinity chromatography techniques. The proteinase has a molecular weight of approx. 28 000 and it is inhibited by alpha 2-macroglobulin, alpha 1-antitrypsin, C-1 inactivatory, soybean trypsin inhibitor and diisopropyl fluorophosphate. 2njection of 1 ng of purified proteinase into rabbit skin induces polymorphonuclear leukocyte infiltration of the cutis. Inhibition of enzyme activity with diisopropyl fluorophosphate inhibits the chemotactic effect. Addition of 0.2 microgram/ml of purified proteinase to fibroblast cultures kills the cells within minutes. This proteinase may play a significant role in modulating the inflammatory response after cellular injury.
利用凝胶过滤和亲和层析技术，已从人皮肤中分离出一种在生理pH值下具有活性的蛋白酶（EC 3.4.-.-）。该蛋白酶的分子量约为28000，可被α2-巨球蛋白、α1-抗胰蛋白酶、C1灭活剂、大豆胰蛋白酶抑制剂和二异丙基氟磷酸酯抑制。将1纳克纯化的蛋白酶注射到兔皮肤中会引起皮肤的多形核白细胞浸润。用二异丙基氟磷酸酯抑制酶活性可抑制趋化作用。向成纤维细胞培养物中添加0.2微克/毫升纯化的蛋白酶会在几分钟内杀死细胞。这种蛋白酶可能在调节细胞损伤后的炎症反应中起重要作用。
