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Figure 3 | Parasites & Vectors

Figure 3

From: Modulation of phosphofructokinase (PFK) from Setaria cervi, a bovine filarial parasite, by different effectors and its interaction with some antifilarials

Figure 3

Effect of ADP on the rate of PFK catalysed reaction under inhibitory (A and B) and optimal (C and D) substrate concentrations. Figure 3A. Effect of ADP 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 ADP. Figure 3B. Double reciprocal plot of the data of Figure 3A. Figure 3C. Effect of ADP 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 ADP. Figure 3D. Double reciprocal plot of the data of Figure 3C.

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