Abstrait

Studies on Effect of Drugs on Human Liver Glucoamylase

A. L. Thombare and N. B. Patil

Human liver glucoamylase was purified using four convenyional steps viz Fractional precipitation with ammonium sulfate, ion exchange chromatography on DEAE cellulose, molecular sieving on bio gel P-100 and poly acrylamide gel electrophpresis technique, even though the molecular size of the isoenzymes was very close to each other. Human liver glucoamyla se was immobilized on CNBr activated agaropection. Human liver glucoamylase was characterized and showed pH optima of 4.4 and 5.6; temperature optima 50 o C and 45 o C; Km characteristics towards starch 26.6 mg /mL and 15.4 mg/mL for free and immobilized. The drug penicillin competitively inhibited the human liver glucoamylase activity while streptomycin accelerated the activity of reaction