从小鼠肝微粒体中纯化和鉴定一种新型的46.5千道尔顿酯酶
Purification and characterization of a novel 46.5-kilodalton esterase from mouse hepatic microsomes.
作者信息
Watanabe K, Kayano Y, Matsunaga T, Yamamoto I, Yoshimura H
机构信息
Department of Hygienic Chemistry, Faculty of Pharmaceutical Sciences, Hokuriku University, Kanazawa, Japan.
出版信息
Biochem Mol Biol Int. 1993 Sep;31(1):25-30.
A novel membrane-bound esterase was purified from mouse hepatic microsomes. The purified protein (ES46.5K) showed a single protein-staining band on sodium dodecyl sulfate-polyacrylamide gel with a minimum molecular weight of 46.5 Kdalton. ES46.5K possessed esterase activity toward 11-acetoxy-delta 8-tetrahydrocannabinol (11-OAc-delta 8-THC) (27.1 mumol/min/mg protein) and p-nitrophenylacetate (119 mumol/min/mg protein), and these activities were 38 and 47 times, respectively, as high as those of microsomes. The N-terminal amino acid sequence of the protein was as follows: G-K-T-I-S-L-L-I-S-V-V-L-V-A-Y-Y-L-Y-I. This sequence has no homology to those of the known carboxylesterases, indicating that this enzyme is a novel type of esterase bound to the microsomal membrane.
从小鼠肝微粒体中纯化出一种新型膜结合酯酶。纯化后的蛋白质（ES46.5K）在十二烷基硫酸钠-聚丙烯酰胺凝胶上呈现出一条单一的蛋白染色带，最低分子量为46.5千道尔顿。ES46.5K对11-乙酰氧基-δ8-四氢大麻酚（11-OAc-δ8-THC）（27.1微摩尔/分钟/毫克蛋白质）和对硝基苯乙酸酯（119微摩尔/分钟/毫克蛋白质）具有酯酶活性，这些活性分别是微粒体活性的38倍和47倍。该蛋白质的N端氨基酸序列如下：G-K-T-I-S-L-L-I-S-V-V-L-V-A-Y-Y-L-Y-I。此序列与已知羧酸酯酶的序列无同源性，表明该酶是一种新型的与微粒体膜结合的酯酶。
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