Järvinen M, Hopsu-Havu V K
Acta Chem Scand B. 1975;29(6):671-6. doi: 10.3891/acta.chem.scand.29b-0671.
The cathepsin B1-like, alpha-N-benzoyl-DL-arginine-2-naphthylamide (BANA) hydrolyzing activity of rat skin extract was studied. The enzyme was extracted into low ionic strength buffers, and was activated by dithiothreitol, EDTA and KCN. Incubation of the extract at acidic pH resulted in a 3.6-fold increase in its BANA hydrolase activity. The presence of inhibitor(s) of BANA hydrolase in the skin extract was indicated by the non-linearity of the activity/enzyme concentration curve and by Sephadex G-100 gel chromatography, which also caused separation of several other skin proteases.
对大鼠皮肤提取物的组织蛋白酶B1样α-N-苯甲酰-DL-精氨酸-2-萘酰胺(BANA)水解活性进行了研究。该酶被提取到低离子强度缓冲液中,并被二硫苏糖醇、EDTA和KCN激活。提取物在酸性pH下孵育导致其BANA水解酶活性增加3.6倍。活性/酶浓度曲线的非线性以及Sephadex G-100凝胶色谱表明皮肤提取物中存在BANA水解酶抑制剂,该凝胶色谱还导致了其他几种皮肤蛋白酶的分离。