Preparation of homogeneous juvenile hormone specific esterase from the haemolymph of the tobacco hornworm, Manduca sexta

Thomas A. Coudron, Peter E. Dunn, Hidelisa L. Seballos, Robert E. Wharen, Larry L. Sanburg, John H. Law

Research output: Contribution to journalArticlepeer-review

37 Scopus citations

Abstract

Juvenile hormone specific esterase has been purified to homogeneity from the haemolymph of Manduca sexta by a combination of gel permeation, ion exchange and hydroxylapatite chromatography. The pure esterase has a molecular weight of 68,000 and consists of a single peptide chain. Juvenile hormone specific esterase hydrolyzes JH I at about twice the rate as JH III, has appreciable activity against methyl farnesenate, but does not hydrolyze 1-naphthyl acetate. The homogeneous enzyme is stable for several months when stored at low temperature.

Original languageEnglish (US)
Pages (from-to)453-461
Number of pages9
JournalInsect Biochemistry
Volume11
Issue number4
DOIs
StatePublished - 1981

Keywords

  • Juvenile hormone
  • Manduca sexta
  • esterase
  • haemolymph

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