Esterase activity in rat hepatocytes.

Hydrolysis of acetylsalicylate, benorylate, phenetsal, fluazifop butyl and paraoxon has been studied with freshly isolated rat hepatocytes maintained as a monolayer. Acetylsalicylate and paraoxon were the poorest substrates for hydrolysis whereas benorylate was hydrolysed one hundred times faster. Phenetsal and fluazifop butyl were both hydrolysed at one-tenth of the rate of benorylate. Inhibitor studies with paraoxon, BNPP and physostigmine indicated the involvement of different carboxylesterase isozymes. Studies with acetylsalicylate indicated that uptake of the substrate into the hepatocyte may influence the rate of formation of the hydrolysis product. Studies of hydrolysis in hepatocytes more closely reflect in vivo hepatic hydrolysis than subcellular fractions as cytosolic and microsomal esterases can act in parallel.