Characterization and affinity purification of juvenile hormone esterase from Bombyx mori |
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| Authors: | Shiotsuki T Bonning B C Hirai M Kikuchi K Hammock B D |
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| Institution: | Department of Insect Physiology and Behavior, National Institute of Sericultural and Entomological Science, Tsukuba, Ibaraki, Japan. shiotsuk@nises.affrc.go.jp |
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| Abstract: | 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. |
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