牛晶状体中性蛋白酶制剂中两种蛋白水解活性的差异抑制
Differential inhibition of two proteolytic activities in bovine lens neutral-proteinase preparations.
作者信息
Wagner B J, Margolis J W, Abramovitz A S, Fu S C
出版信息
Biochem J. 1985 Jun 1;228(2):517-9. doi: 10.1042/bj2280517.
Abstract
Hydrolysis of carbobenzoxy-Leu-Leu-Glu 2-naphthylamide by bovine lens neutral-proteinase preparations is not affected by the esterase inhibitor di-isopropyl fluorophosphate, whereas hydrolysis of carbobenzoxy-Gly-Gly-Leu p-nitroanilide is completely inhibited. Hydrolysis of alpha-crystallin, a lens structural protein, can be inhibited by only 50% after prolonged treatment with di-isopropyl fluorophosphate. These data suggest that the lens neutral-proteinase preparation contains at least two enzymes, one of which may be a serine proteinase. This may account, in part, for the previously observed complex response of the preparation to inhibitors.
摘要
牛晶状体中性蛋白酶制剂对苄氧羰基 - 亮氨酰 - 亮氨酰 - 谷氨酸2 - 萘酰胺的水解不受酯酶抑制剂二异丙基氟磷酸的影响，而苄氧羰基 - 甘氨酰 - 甘氨酰 - 亮氨对硝基苯胺的水解则被完全抑制。经二异丙基氟磷酸长时间处理后，晶状体结构蛋白α - 晶状体蛋白的水解仅能被抑制50%。这些数据表明，晶状体中性蛋白酶制剂至少含有两种酶，其中一种可能是丝氨酸蛋白酶。这可能部分解释了之前观察到的该制剂对抑制剂的复杂反应。
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