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 language | English (US) |
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Pages (from-to) | 453-461 |
Number of pages | 9 |
Journal | Insect Biochemistry |
Volume | 11 |
Issue number | 4 |
DOIs | |
State | Published - 1981 |
Keywords
- Juvenile hormone
- Manduca sexta
- esterase
- haemolymph