Purification and some properties of streptococcal NAD-glycohydrolase
Open Access
- 1 February 1996
- journal article
- research article
- Published by Oxford University Press (OUP) in FEMS Microbiology Letters
- Vol. 136 (1) , 71-78
- https://doi.org/10.1016/0378-1097(95)00495-5
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 VSGKEGKKSDVKYEMTKVMEANATSS-KEDKHVMHTLDKVM. According to serological methods, the purified enzyme of group C streptococci was identical to the group A enzyme showing a specific activity of 10000000 U mg−1. It did not attack NADH, NADP or NADPH. In addition, a streptodornase was isolated having an N-terminal sequence of KTVSVNQTYGE.Keywords
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