Purification and some properties of streptococcal NAD-glycohydrolase.
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.
Gerlach
D
D
Friedrich-Schiller-Universitat Jena, Institut fur Experimentelle Mikrobiologie, Germany.
Ozegowski
J H
JH
Gunther
E
E
Vettermann
S
S
Kohler
W
W
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D003850:Deoxyribonuclease I / Q000235:genetics / Q000302:isolation & purification; D005779:Immunodiffusion; D007700:Kinetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009244:NAD+ Nucleosidase / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D013291:Streptococcus / Q000201:enzymology* / Q000235:genetics; D013297:Streptococcus pyogenes / Q000201:enzymology / Q000235:genetics
D003850:Deoxyribonuclease I; D009244:NAD+ Nucleosidase