Mammalian liver microsomal carboxylesterases comprise a family of isozymes, few of which have been purified or studied at the molecular level. These enzymes play an important role in the metabolism of drugs, lipids and other xenobiotics. The purpose of this study was to establish conditions for the selective solubilization of these microsomal enzymes. Solubilization of mouse liver microsomal carboxylesterase was examined with Triton X-100, Lubrol PX, octyl glucoside and 3-(3'-cholamidopropyl)-dimethylammonio-1-propane sulphonate (CHAPS). The solubilized esterase activities were assayed with p-nitrophenyl acetate (p-NpAc), α-naphthyl acetate (α-NA) and malathion. Triton X-100, Lubrol PX and CHAPS solubilized > 90% of the esterase activity acting on p-NpAc and malathion at 0.05-0.10% concentrations, whereas esterase activity acting on α-NA was released at 0.3-1.0% concentrations. Octyl glucoside caused maximum solubilization of esterase activity acting on malathion at 0.3% and p-NpAc or α-NA at > 1%. These detergents solubilized the membrane-bound esterases to varying degrees depending on the concentrations and the substrate used. Octyl glucoside and CHAPS are effective detergents for solubilization due to their high critical micellar concentrations, selectivity, maintenance of high esterase activities and ease of removal by dialysis.
|Original language||English (US)|
|Number of pages||4|
|State||Published - 1997|
ASJC Scopus subject areas
- Pharmaceutical Science