[Comparative studies of the properties of aldolase isoenzymes A-C in normal rabbit brain and in skeletal muscles from rabbits with E-avitaminosis dystrophy].

By means of fructose-1,6-diphosphate selective elution of aldolase isoenzymic forms from the phosphocellulose column the izoenzyme AC3 was isolated preparatively from the muscles rabbits with experimental E-avitaminosis muscular dystrophy. The specific activity of aldolase A4 and AC3 with pathology differs from that at normal state by fructose-1,6-diphosphate and fructose-1-monophosphate. As to the electrophoretic activity the isoenzymes A4 and AC3 are similar to the same isoforms at normal state. The values of the Michaelis constants and maximal rate are determined for aldolases A4, AC3 and C4 at normal state and for A4 and AC3 with E-avitaminosis. Differences in these parameters are found relative to two substrates for A4 aldolase and AC3-hybrid at normal state and with dystrophy.