[Solubilization and several properties of NAD-glucohydrolase isolated from rabbit heart].
Methods of isolation of NAD-glucohydrolase from the fraction of heart microsomes were searched for. NAD-glucohydrolase proved to pass into a soluble state under the effect of phospholipase A, triton X-100 and Na cholate. NAD-glucohydrolase was found to possess peculiar properties; it reversibly became denatured under the effect of 6M urea, but failed to become inactivated with own substrate (NAD) at pH 8.0. In case of  NAD-ases isolated from other sources the reversible denaturation by means of urea as a rule correlated with the enzyme inactivation in the presence of NAD at pH 8.0.
D000818:Animals; D002384:Catalysis; D002793:Cholic Acids; D005947:Glucose; D006863:Hydrogen-Ion Concentration; D008861:Microsomes / Q000201:enzymology*; D009206:Myocardium / Q000201:enzymology / Q000648:ultrastructure*; D009699:N-Glycosyl Hydrolases / Q000302:isolation & purification; D009243:NAD; D010740:Phospholipases; D011092:Polyethylene Glycols; D011489:Protein Denaturation; D011817:Rabbits; D012964:Sodium; D012995:Solubility; D014508:Urea
D002793:Cholic Acids; D009243:NAD; D011092:Polyethylene Glycols; D014508:Urea; D012964:Sodium; D010740:Phospholipases; D009699:N-Glycosyl Hydrolases; D005947:Glucose
Soliubilizatsiia i nekotorye svoĭstva NAD-gliukogidrolazy, vydelennoĭ iz serdtsa krolika