Characterization and affinity purification of juvenile hormone esterase from Bombyx mori

Takahiro Shiotsuki, Bryony C. Bonning, Makoto Hirai, Kyoko Kikuchi, Bruce D. Hammock

Research output: Contribution to journalArticle

27 Scopus citations

Abstract

Juvenile hormone esterase (JHE) from hemolymph of the silkworm moth Bombyx mon 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.

Original languageEnglish (US)
Pages (from-to)1681-1687
Number of pages7
JournalBioscience, Biotechnology and Biochemistry
Volume64
Issue number8
StatePublished - Aug 2000

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Keywords

  • Affinity purification
  • Bombyx mori
  • Juvenile hormone esterase
  • Transition-state analog
  • Trifluoromethyl ketone

ASJC Scopus subject areas

  • Food Science
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biotechnology
  • Chemistry (miscellaneous)
  • Applied Microbiology and Biotechnology
  • Bioengineering

Cite this

Shiotsuki, T., Bonning, B. C., Hirai, M., Kikuchi, K., & Hammock, B. D. (2000). Characterization and affinity purification of juvenile hormone esterase from Bombyx mori. Bioscience, Biotechnology and Biochemistry, 64(8), 1681-1687.