Purification and subunit structure of rat mammary gland acetyl coenzyme A carboxylase.
1. Acetyl coenzyme A carboxylase from lactating rat mammary gland has been purified to apparent homogeneity. 2. The purified enzyme has the following characteristics: (a) its specific activity approaches 15 units/mg of protein, (b) the sedimentation constants of the protomeric and polymeric forms of the enzyme are 12 to 13 S and greater than or equal to 40 S, respectively, (c) the polymeric form of the enzyme shows filamentous structures in the electron microscope, and (d) the polypeptide(s) arising from its dissociation reveals a single major component of Mr = 240,000 to 260,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. 3. The enzyme contains 1 mol of biotin and approximately 6 mol of phosphate/240,000 g of protein.
Purification and subunit structure of rat mammary gland acetyl coenzyme A carboxylase. 1. Acetyl coenzyme A carboxylase from lactating rat mammary gland has been purified to apparent homogeneity. 2. The purified enzyme has the following characteristics: (a) its specific activity approaches 15 units/mg of protein, (b) the sedimentation constants of the protomeric and polymeric forms of the enzyme are 12 to 13 S and greater than or equal to 40 S, respectively, (c) the polymeric form of the enzyme shows filamentous structures in the electron microscope, and (d) the polypeptide(s) arising from its dissociation reveals a single major component of Mr = 240,000 to 260,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. 3. The enzyme contains 1 mol of biotin and approximately 6 mol of phosphate/240,000 g of protein.