Crystallization of Rat Liver Aldolase*

Publisher Website
Google Scholar
Abstract
The ratios of activities of aldolase [fructose-1, 6-diphosphate D-glyceraldehyde-3-phosphate-lyase, for fructose 1,6-diphosphate and fructose 1-phosphate in many strains of Yoshida ascites hepatomas were different from that of normal rat liver. The enzyme in rapidly growing rat hepatoma seemed to be the muscle-type rather than the livertype. The observation on the inhibition by adenine nucleotides and activity changes due to limited hydrolysis by carboxypeptidase suggest the occurrence of both types of aldolase in slowly growing rat hepatoma[long dash]Morris minimum deviation hepatoma. To elucidate whether or not variant forms of aldolase of the liver-type exist in rat hepatoma in addition to the muscle-type enzyme, it was necessary to obtain both types of rat aldolase in the pure crystalline state. This communication describes the purification and crystallization of rat liver aldolase.