Purification and kinetics of juvenile hormone esterase from the cabbage looper, Trichoplusia ni (Hubner)

Document Type

Article

Publication Date

1-1-1983

Abstract

A method for purifying juvenile hormone esterase from the haemolymph of Trichopulsia ni (Hubner) was developed. The procedure resulted in a single protein band when electrophoresed on SDS-polyacrylamide gels. The enzyme consisted of a single polypeptide chain of mol. wt 48,000 as determined by gel electrophoresis and gel filtration chromatography. Enzyme activity was stable in 40% sucrose for more than 5 months, and unstable when exposed to charged environments at low enzyme concentration. The enzyme possessed apparent Km values of 1.13 × 10-6 and 0.402 × 10-6 M for JH I and JH III, respectively. © 1983.

Publication Source (Journal or Book title)

Insect Biochemistry

First Page

129

Last Page

136

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