Kinetic Study of Acetyle CoA Carboxylase-1purified From Serum of Premenopausal Breast Cancer Women

Abstract

Acetyle CoA Carboxylase-1 was purified from sera of premenopausal women with breast cancer( before Mastectomy or treatment ) by Gel Filtration using Sephadex G-100 and by Ion Exchange using DEAE-Cellulose A-50, also the molecular weight was estimated by the Acrylamide Electrophoresis in the absence of denaturing elements . The result showed that a single band was obtained at 220KD by Gel Filtering while Ion Exchange showed one band at 200KD. The optimum temperature of purified Acetyle CoA Carboxylase-1 was 40 °C, optimal pH at 7.5 and the optimum substrate concentration at 1.8mM. Michaelis-Menten constant (km) was 0.37Mm and Velocity Maximum (Vmax) was 25mM.min−1 The Activation energy(Ea) was 28 KJ/mol.