Fujimura S, Nakamura T, Pulverer G
Zentralbl Bakteriol Mikrobiol Hyg A. 1986 Apr;261(2):133-9. doi: 10.1016/s0176-6724(86)80028-1.
From the cell extract of Corynebacterium matruchotii strain ATCC 14266, a peptidase could be isolated and purified, increasing the specific activity 267 times. This enzyme with a molecular weight of 60,000 was completely inactivated by heating at 50 degrees C for 20 min, its optimum pH was found to be pH 7.5 and the isoelectric point was 4.1. The peptidase was inhibited by diisopropylfluorophosphate, phenylmethanesulfonyl fluoride, tosyl-L-lysine chloromethyl ketone, chymostatin and urea. Among various synthetic substrates tested, only benzoyl-L-arginine-p-nitroanilide and benzoyl-L-arginine ethylester were found to be hydrolyzed by this enzyme. Several proteins investigated were not hydrolyzed, but the enzyme inactivated a peptidic staphylococcal bacteriocin.
从粘液棒状杆菌ATCC 14266菌株的细胞提取物中，可以分离并纯化出一种肽酶，其比活性提高了267倍。这种分子量为60,000的酶在50℃加热20分钟后完全失活，其最适pH值为7.5，等电点为4.1。该肽酶受到二异丙基氟磷酸、苯甲基磺酰氟、甲苯磺酰-L-赖氨酸氯甲基酮、抑肽酶和尿素的抑制。在测试的各种合成底物中，发现只有苯甲酰-L-精氨酸对硝基苯胺和苯甲酰-L-精氨酸乙酯能被该酶水解。所研究的几种蛋白质未被水解，但该酶使一种肽类葡萄球菌细菌素失活。
