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Journal of Lipid Research, Vol 21, 484-488, Copyright © 1980 by Lipid Research, Inc.

ARTICLES

A rapid assay of acyl-coenzyme A:lysolecithin acyltransferase activity

K Hayase, S Parthasarathy, CM Eppler and WJ Baumann

A simple and rapid procedure for the assay of acyl-coenzyme A:1-acyl-sn- glycero-3-phosphocholine acyltransferase (lysolecithin acyltransferase, LLAT [EC 2.3.1.23]) activity in crude enzyme preparations is described. The incubation system utilizes lysolecithin and [1-14C]-oleoyl-coenzyme A as substrates. Labeled fatty acid released due to accompanying acyl- coenzyme A hydrolase [EC 3.1.2.2]activity is first removed by di- isopropyl ether extraction. The labeled lecithin produced due to LLAT action is then quantitatively recovered by partition of the incubation medium with di-isopropyl ether-n-butanol 60:40 (v/v). Selective extraction of the labeled lecithin formed and avoidance of customary thin-layer chromatographic isolation procedures permits assay of LLAT activity with excellent accuracy at a substantial saving of time. The entire assay can be completed in less than 30 min as compared to 2-3 hrs when following conventional procedures.
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