title: Factors affecting deoxycholate inactivation and Mg++ reactivation of Bacillus megaterium KM membrane nicotinamide adenine dinucleotide (reduced form) oxidase.
abstract: Decay of the reduced nicotinamide adenine dinucleotide oxidase of Bacillus megaterium KM membranes was prevented by storage in 10% (v/v) glycerol or 0.4% bovine serum albumin. Differential rates of solubilization of components of the oxidase system by 0.4% deoxycholate was demonstrable at 4 C. The amount of Mg(++) necessary for maximal oxidase reactivation increased with increasing amounts of deoxycholate-inactivated oxidase. Mg(++) activation of deoxycholate-inactivated oxidase was partially temperature-dependent. Maximal activation was observed at 37 C, but only partial activation took place at 4 C. A small amount of deoxycholate was required for Mg(++) activation of deoxycholate-inactivated oxidase. Two pH optima were found for Mg(++) activation of deoxycholate-inactivated oxidase, pH 5.3 and 7.3. Significant amounts of activation of the inactive oxidase occurred in the absence of Mg(++) with an optimum at pH 5.0, with essentially no Mg(++)-independent activation demonstrable at pH 7.0.
mesh_terms: D001410:Bacillus megaterium / Q000201:enzymology*; D001647:Bile Acids and Salts / Q000378:metabolism*; D002462:Cell Membrane / Q000201:enzymology*; D004789:Enzyme Activation; D006863:Hydrogen-Ion Concentration; D008274:Magnesium / Q000378:metabolism*; D010088:Oxidoreductases / Q000378:metabolism*; D013696:Temperature
chemical_list: D001647:Bile Acids and Salts; D010088:Oxidoreductases; D008274:Magnesium