[Various regulatory properties of fructose-1,6-diphosphatase of the rat liver under normal conditions and in experimental autoimmune cardiomyopathy].

An increase in fructose-1,6-biphosphatase activity in liver tissue of rats with experimental autoimmune cardiomyopathy was observed. At certain concentrations of EDTA and Mg2+ the AMP-inhibition curves exhibited an intermediate plateau, which appear under different experimental, normal and pathological conditions. The occurrence of complex kinetic curves could be attributed to simultaneous existence of several enzymatic forms differing in the "structural" sites with tightly bound metals, which defines the differences in the kinetic cooperativity and sensitivity to AMP inhibition.