Kinetic analysis of a general model of activation of aspartic proteinase zymogens involving a reversible inhibitor. I. Kinetic analysis

Figures & data

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Figure 1 (A) Time course of [E] and [Z] according to Equations (13) and (15) and from the numerical integration of the set of differential Equations 4-8. (B) Time course of [Z*] and [EI] [EI] according to Equations (16) and (18) and from the numerical integration of the set of differential Equations 4-8. The values of the equilibrium constants, rate constants and initial concentrations in (A) and (B) were: and In each case the progress curves from the equation and from the simulation overlap in the scale used.

Figure 2 Time course of [E]_a, according to Equation (19), for the same set of values of the equilibrium constants, rate constants and initial concentrations were the same as in Fig. 1.

Figure 3 Effect of [I]₀ on the time course of [E]_a at fixed [Z]₀- and [E]₀-values according to Equation (19). For each progress curve the set of values of the equilibrium constants, rate constants, [Z]₀ and [E]₀ are the same as in Fig. 1. The [I]₀-values used in the different progress curves were (mM): 0, 0.05, 1, 5, 10 and 50.

Figure 4 Effect of [E]₀ on the time course of [E]_a at fixed [Z]₀- and [I]₀-values according to Equation (19). For each progress curve the set of values of the equilibrium constants, rate constants, [Z]₀ and [I]₀ are the same as in Fig. 1. The [E]₀-values used in the different progress curves were (nM): 0, 20, 40, 60, 80 and 100.

Figure 5 Effect of [Z]₀ on the time course of [E]_a at fixed [I]₀- and [E]₀-values according to Equation (19). For each progress curve the set of values of the equilibrium constants, rate constants, [I]₀ and [E]₀ are the same as in Fig. 1. The [Z]₀-values used in the different progress curves were (μM): 1, 1.05, 1.10, 1.20, 1.25 and 1.40.