Abstract
We report the first complete structural characterization of a metabolically-produced halocarbon radical bound to a phospholipid. Human cytochrome P-450 and NADPH cytochrome P-450 reductase were reconstituted into vesicles composed of dioleoylphosphatidylcholine and egg phosphatidylethanolamine. The vesicles were incubated under argon with NADPH and [ 14C]-halothane (1-[ 14C]-2-bromo-2-chloro-1,1,1-trifluoroethane), the dioleoylphosphatidylcholine fraction was isolated and subjected to transesterification. Separation of the resulting fatty acid methyl esters resulted in one radioactive fraction which gas chromatography-mass spectrometry revealed to be a mixture of 9- and 10-(1-chloro-2,2,2-trifluoroethyl)-stearate methyl ester.
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More From: Biochemical and Biophysical Research Communications
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