Abstract
Abstract A heat-stable soluble enzyme has been isolated from bovine cardiac muscle which catalyzes the reduction of palmityl coenzyme A and stearyl coenzyme A to the corresponding fatty aldehyde. The enzyme has been purified about 480-fold over the original 105 x g supernatant fraction by heating, ammonium sulfate fractionation, and gel filtration chromatography. It has a molecular weight in the range 85,000 to 95,000 and requires NADH as a cofactor. A pH optimum in the range 7.0 to 7.5 has been demonstrated. Palmityl-CoA and stearyl-CoA are substrates for the enzyme. The aldehyde product has been verified by chromatography and conversion to derivatives.
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