Abstract
A novel membrane-bound esterase was purified from hepatic microsomes of male ddN mice using ω-aminooctyl Sepharose-4B, DEAE-5PW, CM-Sephadex C-50 and/or hydroxylapatite column chromatographies. The purified enzyme (ES46.5K) showed a single band on a sodium dodecylsulfate-polyacrylamide gel with a mimimum molecular weight of 46.5 Kd. The N-terminal amino acid sequence of the enzyme had no homology to those of known carboxylesterases. ES46.5K exhibited esterase activities toward 11-acetoxy derivatives of tetrahydrocannabinol (THC), whereas the enzyme did not hydrolyze phenolic acetates of cannabinoids (Δ8-THC, Δ9-THC and cannabidiol) except for 1-acetyl-cannabinol. ES 46.5K also possessed esterase activity toward p-nitrophenylacetate, 1-naphtylacetate and 2-acetylaminofluorene. Emulgen 911 and deoxycholate affected differently on the esterase activity of ES46.5K and carboxylesterase purified from porcine liver. Immuno-reactive protein to antibody against ES46.5K was present in hepatic microsomes from mice and rabbits, but not those from rats, guinea pigs and monkeys. The present study demonstrates that mouse hepatic microsomes contain a novel type of esterase having molecular weight of 46.5 Kd and high catalytic activity toward 11-hydroxy-esters of cannabinoids.
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