Solubiliztion and Partial Characterization of Alkylglycerol Monooxygenase from the Liver Mkcosomes

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Abstract
The enzyme alkylglycerol monoooxygenase was solubilized with 2% of Triton X-100 and partially purified .apprx. to 83-fold with a 36% yield after a procedure which included 6-aminohexyl-Sepharose and DEAE-cellulose column chromatography, followed by a sucrose density gradient centrifugation. The MW of the native form was estimated to be .apprx. 400,000 as judged by Sepharose 6B column chromatography in the presence of Triton X-100. The enzyme had a pH optimum near 8.5 and a Km of 0.66 mM for 1-O-hexadecylglycerol. The microsomal alkylglycerol monooxygenase was stimulated by Triton X-100, but did not affect kinetically the initial velocity except to maintain it for a much longer period of time. The purified enzyme required absolutely both molecular O2 and reduced pteridine as an electron donor. Furthermore, reduced glutathione and phospholipids were necessary for expression of full enzyme activity. N-Ethylmaleimide and p-chlormercuribenzoate significantly inhibited the enzyme activity, suggesting that alkylglycerol monooxygenase is a -SH enzyme.

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