NADH-dependent methemoglobin reductase in hemolysates and in partially purified preparations was tested for thermostability and coenzyme dependency. Thermoinactivation of the coenzyme was prevented by NAD 10-4m, while NADP had no effect. NAD glycohydrolase produced a decrease in methemoglobin reductase activity and a typical change in electrophoretic pattern. No change in molecular weight as detected by electrophoresis on polyacrylamide at various concentrations was found among the multiple bands.
ASJC Scopus subject areas
- Molecular Biology