链球菌NAD-糖水解酶的纯化及其某些性质

Purification and some properties of streptococcal NAD-glycohydrolase.

作者信息

Gerlach D, Ozegowski J H, Gunther E, Vettermann S, Kohler W

机构信息

Friedrich-Schiller-Universitat Jena, Institut fur Experimentelle Mikrobiologie, Germany.

出版信息

FEMS Microbiol Lett. 1996 Feb 1;136(1):71-8. doi: 10.1016/0378-1097(95)00495-5.

DOI:10.1016/0378-1097(95)00495-5

PMID:8919458

Abstract

NAD-glycohydrolase (NADase) was purified from culture supernatant fluids of group C streptococci by adsorption on silica gel, chromatography on hydroxyapatite and ion exchange on Mono S column. After inactivation of a chymotrypsin-like protease, a homogeneous enzyme was isolated with an N-terminal sequence of VSGKEGKKSDVKYEMTKVMEANATSSKEDKHVMHTLDKVM. According to serological methods, the purified enzyme of group C streptococci was identical to the group A enzyme showing a specific activity of 10 000 000 U mg-1. It did not attack NADH, NADP or NADPH. In addition, a streptodornase was isolated having an N-terminal sequence of KTVSVNQTYGE.

摘要

通过硅胶吸附、羟基磷灰石层析和Mono S柱离子交换，从C组链球菌的培养上清液中纯化出烟酰胺腺嘌呤二核苷酸糖水解酶（NADase）。在一种类胰凝乳蛋白酶的蛋白酶失活后，分离出一种均一的酶，其N端序列为VSGKEGKKSDVKYEMTKVMEANATSSKEDKHVMHTLDKVM。根据血清学方法，C组链球菌的纯化酶与A组酶相同，比活性为10 000 000 U mg-1。它不作用于NADH、NADP或NADPH。此外，还分离出一种链道酶，其N端序列为KTVSVNQTYGE。