Shiotsuki T, Bonning B C, Hirai M, Kikuchi K, Hammock B D
Department of Insect Physiology and Behavior, National Institute of Sericultural and Entomological Science, Tsukuba, Ibaraki, Japan.
Biosci Biotechnol Biochem. 2000 Aug;64(8):1681-7. doi: 10.1271/bbb.64.1681.
Juvenile hormone esterase (JHE) from hemolymph of the silkworm moth Bombyx mori was characterized for substrate specificity and inhibitor sensitivity. B. mori JHE hydrolyzed the juvenile hormone surrogate substrate methyl n-heptylthioacetothioate (HEPTAT) more efficiently than p-nitrophenyl acetate and 1-naphthyl acetate substrates widely used to assay total carboxylesterase activity. B. mori JHE was sensitive to 3-octylthio-1,1,1-trifluoro-2-propanone (OTFP), which was developed as a selective inhibitor for lepidopteran JHE, and relatively insensitive to diisopropyl fluorophosphate (DFP), an inhibitor of serine esterases but not of all JHEs. Affinity purification with a trifluoromethyl ketone ligand was more efficient for purification of B. mori JHE than DEAE ion exchange chromatography.
对家蚕蛾血淋巴中的保幼激素酯酶（JHE）的底物特异性和抑制剂敏感性进行了表征。家蚕JHE水解保幼激素替代底物正庚硫基乙酰硫代乙酸甲酯（HEPTAT）的效率高于用于测定总羧酸酯酶活性的对硝基苯乙酸酯和1-萘乙酸酯底物。家蚕JHE对作为鳞翅目JHE选择性抑制剂开发的3-辛硫基-1,1,1-三氟-2-丙酮（OTFP）敏感，而对丝氨酸酯酶抑制剂二异丙基氟磷酸酯（DFP）相对不敏感，DFP并非对所有JHE都有抑制作用。用三氟甲基酮配体进行亲和纯化比对家蚕JHE进行DEAE离子交换色谱纯化更有效。
