Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
Genetic identification of rat liver carboxylesterases isolated in different laboratories☆
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The role of carboxylesterases in therapeutic interventions of nerve agent poisoning
2020, Handbook of Toxicology of Chemical Warfare AgentsThe Role of Carboxylesterases in Therapeutic Intervention of Nerve Gases Poisoning
2015, Handbook of Toxicology of Chemical Warfare Agents: Second EditionRat carboxylesterase ES-4 enzyme functions as a major hepatic neutral cholesteryl ester hydrolase
2011, Journal of Biological ChemistryCitation Excerpt :They are expressed in hepatocytes and hydrolyze a wide variety of lipid ester substrates in vitro. The carboxylesterase family was thought to include over 30 rat liver “carboxylesterases,” but biochemical genetic studies have shown that these enzymes are the products of five major loci in linkage group V (17). These enzymes are designated as ES-2, ES-3, ES-4, ES-10, and ES-15, of which ES-3, ES-4, and ES-10 account for 95% of rat liver microsomal carboxylesterase activity (18).
Role of carboxylesterases in therapeutic intervention of nerve gas poisoning
2009, Handbook of Toxicology of Chemical Warfare AgentsAllosteric kinetics of human carboxylesterase 1: Species differences and interindividual variability
2008, Journal of Pharmaceutical SciencesCitation Excerpt :Imidaprilat formation in RLM and RLC exhibited Michaelis‐Menten kinetics, suggesting that species difference exists. In rat CESs, many isoforms have been identified.22 In the preliminary study, a specific CES inhibitor, BNPP, inhibited the imidaprilat formation in all enzyme sources from rats.
Isolation and characterization of a microsomal acid retinyl ester hydrolase
2005, Journal of Biological ChemistryCitation Excerpt :These results were further supported by the observation that the purified acid retinyl ester hydrolase cross-reacted with a polyclonal anti-ES-10 antibody directed at the C terminus of ES-10. Analytical gel filtration (Fig. 1) showed that the active protein exists as a homotrimeric complex in solution, as had been described for ES-10 previously (26, 27). ES-10 is a member of the nonspecific carboxylesterase supergene family (28) and is able to hydrolyze both xenobiotic and lipid substrates (27).
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This is communication No. 58 of a research programm devoted to the cellular distribution, genetics and regulation of nonspecific esterases.
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Present address:Abt. Medizinische Chemie. Universität Osnabrück, D-4500 Osnabrück, F.R.G.