Properties of the N, N'-dicyclohexylcarbodiimide resistant ATPase OF Streptococcus cremoris

Abstract

1. 1. The specific activity of the membrane-bound ATPase of Streptococcus cremoris HA was 1.30 μmol p i/mg protein/min. 2. 2. K m for ATP as substrate was 0.8 mM. 3. 3. The pH optimum was 8.0 at +37°C. 4. 4. The ATPase was maximally activated with Mg 2+/ATP molar ratio of 1:2. 5. 5. Cations activated the enzyme in order: Mg 2+ > Co 2+ > Mn 2+ > Zn 2+ > Ca 2+ > K 2+ > Na +. 6. 6. The enzyme was inhibited by oligomycin (27–77%), sodium azide (13–33%) and ouabain (15–22%). N, N'-dicyclohexylcarbodiimide had no effect on the enzyme activity.