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• W2022132311 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 microM and 5.7 nmol/min/mgprotein, 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.
• W2022132311 created "2016-06-24" @default.
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• W2022132311 date "2005-04-01" @default.
• W2022132311 modified "2023-09-26" @default.
• W2022132311 title "A spectrophotometric assay for fatty acid amide hydrolase suitable for high-throughput screening" @default.
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• W2022132311 doi "https://doi.org/10.1016/j.bcp.2005.01.012" @default.
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