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EC number: 218-645-3 | CAS number: 2210-79-9
The detoxification of o -CGE (2,3 -epoxypropyl o-tolyl ether) was assessed in vitro in human, rat and mouse subcellular cytosolic and microsome fractions. The rate of o-CGE conjugation to glutathione by glutathione-S-trasnferase and of hydrolysis by Epoxide hydrolase was determined. Generally, conjucation of o-CGE (2,3-epoxypropyl o-tolyl ether ) to glutathione by Gultathione-S-transferase by rodent and human subcellular cytosol fractions from the liver and lung was similar. Hydrolysis of o-CGE by Epoxide hydrolase was the most efficient means of detoxification. Human liver Epoxide hydrolase was approximately 4-10-fold more efficient than rodent Epoxide hydrolase in the hydrolysis of o-CGE. Mouse lung Epoxide hydrolase was approximately 2-fold more efficient compared to human lung Epoxide hydrolase. Generally, rat Epoxide hydrolase was the least efficient in the detoxification of o-CGE.
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