Figure 1
Effect of cAMP on the rate of PFK catalyzed reaction under inhibitory (A and B) and optimal (C and D) substrate concentrations. Figure 1A. Effect of cAMP on the rate of S. cervi PFK catalyzed reaction at fixed inhibitory concentration of ATP (1.0 mM) and low concentration of F-6-P (0.5 mM). Mg2+ concentration was constant (3.3 mM). Enzyme concentration was 6.6 μg/ml. Other conditions were the same as in standard enzyme assay. V and V0 are rates of reaction in the presence and absence of cAMP. Figure 1B. Double reciprocal plot of the data of Figure 1A. Figure 1C. Effect of cAMP on the rate of S. cervi PFK catalyzed reaction at optimal concentrations of substrates (F-6-P, 3.3 mM; ATP, 0.10 mM). Mg2+ concentration was constant (3.3 mM). Enzyme concentration was 6.6 μg/ml. Other conditions were the same as in standard enzyme assay. V and V0 are rates of reaction in the presence and absence of cAMP. Figure 1D. Double reciprocal plot of the data of Figure 1C.