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

doi:10.1016/0020-1790(81)90080-9

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

Neurosurgery

Research output: Contribution to journal › Article › peer-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 language	English (US)
Pages (from-to)	453-461
Number of pages	9
Journal	Insect Biochemistry
Volume	11
Issue number	4
DOIs	https://doi.org/10.1016/0020-1790(81)90080-9
State	Published - 1981

Keywords

Juvenile hormone
Manduca sexta
esterase
haemolymph

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

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.",

keywords = "Juvenile hormone, Manduca sexta, esterase, haemolymph",

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year = "1981",

doi = "10.1016/0020-1790(81)90080-9",

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T1 - Preparation of homogeneous juvenile hormone specific esterase from the haemolymph of the tobacco hornworm, Manduca sexta

AU - Coudron, Thomas A.

AU - Dunn, Peter E.

AU - Seballos, Hidelisa L.

AU - Wharen, Robert E.

AU - Sanburg, Larry L.

AU - Law, John H.

PY - 1981

Y1 - 1981

N2 - 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.

AB - 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.

KW - Juvenile hormone

KW - Manduca sexta

KW - esterase

KW - haemolymph

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