Shibata Y, Miwa Y, Hirai K, Fujimura S
Department of Oral Microbiology, Matsumoto Dental University, Shiojiri, Japan.
Oral Microbiol Immunol. 2003 Jun;18(3):196-8. doi: 10.1034/j.1399-302x.2003.00057.x.
A peptidase hydrolyzed X-Pro-p-nitroanilide was purified from the cell extract of Prevotella intermedia ATCC 25611 by ion-exchange chromatography and hydrophobic interaction chromatography. The purified enzyme exhibited a molecular size of 74 kDa from sodium dodecyl sulfate-polyacrylamide gel electrophoresis and the maximum enzyme activity was found between pH 7.0 and pH 7.5. This peptidase was a serine enzyme and hydrolyzed Lys-Pro-p-nitroanilide, Arg-Pro-p-nitroanilide, and Ala-Pro-p-nitroanilide, but Lys-Ala-p-nitroanilide was not split. The enzyme may be classified as a dipeptidyl peptidase IV.
通过离子交换色谱法和疏水相互作用色谱法，从中间普氏菌ATCC 25611的细胞提取物中纯化出一种水解X-脯氨酰-对硝基苯胺的肽酶。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳显示，纯化后的酶分子大小为74 kDa，最大酶活性出现在pH 7.0至pH 7.5之间。这种肽酶是一种丝氨酸酶，可水解赖氨酸-脯氨酰-对硝基苯胺、精氨酸-脯氨酰-对硝基苯胺和丙氨酸-脯氨酰-对硝基苯胺，但不裂解赖氨酸-丙氨酰-对硝基苯胺。该酶可能被归类为二肽基肽酶IV。
