Abstract
Acetyl CoA carboxylase has been purified from rape seed by a rapid purification procedure consisting of ammonium sulfate fractionation and affinity chromatography on monovalent avidin sepharose and blue sepharose. The final preparation is almost homogeneous when analysed by polyacrylamide gel electrophoresis under denaturing conditions, consistinf of a major polypeptide of 220 000 daltons. Initial homogenization at high dilution is required to isolate this high molecular weight form of the enzyme and the inclusion of standard protease inhibitors is not sufficient to prevent proteolysis. The purified enzyme has a pH optimum of pH 8.5 and apparent K m-values of 74 μm, 38 μm and 3 mM for acetyl CoA, ATP and HCO − 3, respectively.
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