Answer:
The pH on catalysis and activation characteristics of spinach ribulose 1,5-bisphosphate (RuBP) carboxylase were examined at air level of CO2. Catalysis at limiting CO2 was independent of pH over the range of pH 8.2 to 8.8 However, the kinetics of activation and the apparent equilibrium between the activated and inactivated forms of the enzyme were strongly dependent upon the pH and the presence or absence of the substrate RuBP. When incubated at air level of CO2 at pH 8.2 in the absence of RuBP, the enzyme activation state was approximately 75% of that achieved with saturating CO2 at that pH. The extent of activation increased with pH reaching 100% at pH values of 8.6 or higher.
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