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Rat Mammary Acetyl Coenzyme A Carboxylase

I. ISOLATION AND CHARACTERIZATION

From the ¹ From the Biological Research Laboratories, Department of Bacteriology and Botany, and The Biochemistry Committee, Syracuse University, Syracuse, New York, 13210

The isolation of acetyl-CoA carboxylase from lactating rat mammary glands is described. A procedure was used which differs significantly from those employed by others who have isolated this enzyme from animal tissues. The purified enzyme catalyzes the carboxylation of 5.5 µmoles of acetyl-CoA per min per mg of protein under optimum assay conditions. Apparent K_m values were determined for acetyl-CoA, propionyl-CoA, bicarbonate, and ATP (which gave two values). The effects of varying the concentrations of citrate or Mg⁺⁺ yielded sigmoid saturation curves. Phospholipids were found to stimulate the enzyme.

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