Studies on ω-Oxidation of Fatty Acids in vitro

Abstract
ω-Hydroxy fatty acid: NAD oxidoreductase was partially purified from rabbit liver acetone powder. This enzyme had a high substrate specificity on 11-hydroxyundecanoic acid, 11-hydroxycapric acid and 9-hydroxypelargon acid, and showed no activity on 6-hydroxycaproic acid. Ethanol did not act as substrat either. NAD was required for the ω-hydroxyfatty acid: NAD oxidoreductase and NAD could not substitute for NAD. ω-Oxo fatty acid was formed by the dehydrogenation of ω-hydroxy fatty acid. The pH optimum of this enzyme was about 10.5 at 25°C. The enzyme was unstable and inhibited completely by p-chloromercuribenzoate.

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