PURIFICATION AND SOME PROPERTIES OF STREPTOCOCCAL NAD-GLYCOHYDROLASE

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