Desaturation of saturated fatty acids by rat liver microsomes

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Abstract
A method was developed for the rapid determination of the initial velocity of the desaturation of saturated fatty acids. In the reaction, DPNH was a more efficient electron donor than TPNH. Fatdeficient rats have a 2.5‐fold greater level of acyl desaturase per milligram of liver microsomal protein than did animals fed lab chow. Increasing the chain length of the acyl substrate from 10∶0 to 18∶0 increases the rate of monoene formation, but 19∶0 is desaturated at a rate lower than that for 15∶0. The energy of activation (Ea) for the overall desaturation reaction has been determined for 12∶0 through 19∶0. The Ea values for desaturation of 13∶0 and 16∶0 are markedly lowr than for the other acids. An interaction between the alkyl chain of the substrate and polyunsaturated acids of the microsomal membrane‐bound phospholipids is postulated to explain the recurring 3‐carbon pattern of the relative reaction rates of the various acyl substrates.

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