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- W2000927488 abstract "Signalling via the endocannabinoids anandamide and 2-arachidonylglycerol appears to be terminated largely through the action of the enzyme fatty acid amide hydrolase (FAAH). In this report, we describe a simple spectrophotometric assay to detect FAAH activity in vitro using the ability of the enzyme to hydrolyze oleamide and measuring the resultant production of ammonia with a NADH/NAD+-coupled enzyme reaction. This dual-enzyme assay was used to determine Km and Vmax values of 104 μM and 5.7 nmol/min/mg protein, respectively, for rat liver FAAH-catalyzed oleamide hydrolysis. Inhibitor potency was determined with the resultant rank order of methyl arachidonyl fluorophosphonate > phenylmethylsulphonyl fluoride > anandamide. This assay system was also adapted for use in microtiter plates and its ability to detect a known inhibitor of FAAH demonstrated, highlighting its potential for use in high-throughput screening." @default.
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- W2000927488 date "2006-01-01" @default.
- W2000927488 modified "2023-10-16" @default.
- W2000927488 title "Tu-P7:200 Group IVC phospholipase A2 supplies fatty acids utilized for the formation of cholesteryl ester and triacylglycerol in macrophages" @default.
- W2000927488 doi "https://doi.org/10.1016/s1567-5688(06)80904-9" @default.
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