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.
- Juvenile hormone
- Manduca sexta