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  • Title: Purification and some properties of streptococcal NAD-glycohydrolase.
    Author: Gerlach D, Ozegowski JH, Gunther E, Vettermann S, Kohler W.
    Journal: FEMS Microbiol Lett; 1996 Feb 01; 136(1):71-8. PubMed ID: 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.
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