Add time:08/15/2019         Source:sciencedirect.com

Publisher SummaryThis chapter discusses the preparation and purification of methylmalonyl coenzyme A. Two methods have been reported for the preparation of the monothioester of CoA and methylmalonate, including the mixed anhydride method and the reaction catalyzed by propionyl CoA carboxylase. The mixed anhydride of methylmalonie and ethylchlorocarbonic acids is prepared. To a small centrifuge tube containing 1.2 ml of tetrahydrofuran, which has been redistilled within the preceding hour and collected over sodium, is added to 118 mg of dry methylmalonic acid. The latter compound is prepared by saponification of the diethylester and purified by ether extraction and recrystallization from acetone or acetone–petroleum ether. An aliquot of the tetrahydrofuran solution containing 38 μmoles of the mixed anhydride is added to an ice-cold test tube containing 30 μmoles of CoA, 60 mg of potassium bicarbonate, and 3.0 ml of water. The enzymatically prepared compound has been reported to be more completely converted to succinyl CoA by methylmalonyl isomerase than that prepared by the mixed anhydride method. Material active in the isomerase reaction may be obtained by elution of methyl-malonyl CoA from paper chromatograms developed in the ascending direction for 24 h at +2° with a 1:1 mixture of ethanol and 0.1 N sodium acetate, pH 4.5.

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