Figure 3

Simulated results of glycogen cascade system in liver, incorporating glycogen synthase phosphatase inhibition by phosphorylase- a. (A) Fractional modification of enzymes at various concentration of glucose. The sensitivity of the fractional dose-response curve of glycogen synthase (curve a, ~13.6), phosphorylase (curve b, ~6.3), phosphorylase kinase (curve c, ~1.6), CAPK (curve d, ~1.12). (B) Fractional modification of enzymes at various concentrations of cAMP. The sensitivity of fractional dose-response curve of glycogen synthase (curve a, ~6.8), phosphorylase (curve b, ~3.2), phosphorylase kinase (curve c, ~1.6), CAPK (curve d, ~1.12). (C) Fractional modification of enzymes at various concentrations of glucose-6-phosphate. The sensitivity of the fractional dose-response curve of glycogen synthase (curve a, ~14.2) and phosphorylase (curve b, ~6.4). (D) Fractional modification of phosphorylase as a function of glycogen synthase demonstrating reciprocal regulation. The dissociation constant (Kd) of phosphorylase-a binding to glycogen synthase phosphatase is taken as 0.002 μ M.