Figure 2
Effect of AMP on the rate of PFK catalyzed reaction under inhibitory (A and B) and optimal (C) substrate concentrations. Figure 2A. Effect of AMP 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 AMP. Figure 2B. Double reciprocal plot of the data of Figure 2A. Figure 2C: Effect of AMP 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 10.0 μg/ml. Other conditions were the same as in standard enzyme assay.