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Formation of palmitate esters of monohydric short chain alcohols by swine arterial subcellular fractions

1974; Wiley; Volume: 9; Issue: 2 Linguagem: Inglês

10.1007/bf02532131

1558-9307

Robert J. Morin, Thomas J. Ihrig,

Enzyme Catalysis and Immobilization

Abstract Alcohols of 1–5 carbon chain length were esterified with palmitic acid and palmitoyl CoA substrates by swine aortic cytosol, mitochondrial, and microsomal fractions. Esterification of the palmitic acid substrate with ethanol was enhanced by the addition of adenosine 5′‐triphosphate and CoA to the mitochondrial and microsomal fractions. The rate of esterification of ethanol was most rapid in the microsomal fraction and with the palmitoyl CoA substrate. Esterification was linearly related to time of incubation, was optimal at pH 6.8, and could be inactivated by heating at 90 C. Esterification was inactivated by ethanol concentrations above 0.8 M and by lower concentrations of the other alcohols. Rates of esterification were highest with n‐propanol and lowest with tert‐butanol and the pentanols. The formation of cholesteryl esters by the aortic microsomes was inhibited by ethanol and was inversely related to the rate of ethyl palmitate formation.