Epoxide hydrolase activities in Drosophila melanogaster

L. G. Harshman; J. Casas; E. C. Dietze; B. D. Hammock

doi:10.1016/0020-1790(91)90095-V

Epoxide hydrolase activities in Drosophila melanogaster

L. G. Harshman, J. Casas, E. C. Dietze, B. D. Hammock

Biological Sciences

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27 Scopus citations

Abstract

Epoxide hydrolase (EH) activity in Drosophila melanogaster cell fractions was characterized using juvenile hormone (JH III) and cis-stilbene oxide (CSO) as substrates. A comparison of detergents indicated that 0.3% Lubrol PX was relatively effective for solubilizing EH activity from the 20,000 and 100,000 g pellets. The effect of inhibitors, pH, temperature, salt and organic solvents on EH activity depended on the substrate and cell fraction tested, which suggested there were multiple activities present. For initial purification, polyethylene glycol was useful for precipitating EH activity from the 100,000 g supernatant.

Original language	English (US)
Pages (from-to)	887-894
Number of pages	8
Journal	Insect Biochemistry
Volume	21
Issue number	8
DOIs	https://doi.org/10.1016/0020-1790(91)90095-V
State	Published - 1991

Keywords

Drosophila melanogaster
epoxide hydrolase
juvenile hormone

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10.1016/0020-1790(91)90095-V

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title = "Epoxide hydrolase activities in Drosophila melanogaster",

abstract = "Epoxide hydrolase (EH) activity in Drosophila melanogaster cell fractions was characterized using juvenile hormone (JH III) and cis-stilbene oxide (CSO) as substrates. A comparison of detergents indicated that 0.3% Lubrol PX was relatively effective for solubilizing EH activity from the 20,000 and 100,000 g pellets. The effect of inhibitors, pH, temperature, salt and organic solvents on EH activity depended on the substrate and cell fraction tested, which suggested there were multiple activities present. For initial purification, polyethylene glycol was useful for precipitating EH activity from the 100,000 g supernatant.",

keywords = "Drosophila melanogaster, epoxide hydrolase, juvenile hormone",

author = "Harshman, {L. G.} and J. Casas and Dietze, {E. C.} and Hammock, {B. D.}",

note = "Funding Information: Acknowledgements--The juvenile hormone analog inhibitors were generously provided by Istavan Ujvary and Glenn Prestwich. We thank I. Segel for discussion on the use of inhibitors. This work was supported by NIEHS grant ES02710, NSF grant DCB-8518697 and the Superfund Basic Reseach Program (Grant P42-ES04699). Josefina Casas was supported by a Fulbright-Spanish Ministry of Education Fellowship. B. Hammock was supported as a Burroughs Wellcome Toxicology Scholar.",

year = "1991",

doi = "10.1016/0020-1790(91)90095-V",

language = "English (US)",

volume = "21",

pages = "887--894",

journal = "Insect Biochemistry",

issn = "0020-1790",

publisher = "Elsevier Ltd",

number = "8",

}

TY - JOUR

T1 - Epoxide hydrolase activities in Drosophila melanogaster

AU - Harshman, L. G.

AU - Casas, J.

AU - Dietze, E. C.

AU - Hammock, B. D.

N1 - Funding Information: Acknowledgements--The juvenile hormone analog inhibitors were generously provided by Istavan Ujvary and Glenn Prestwich. We thank I. Segel for discussion on the use of inhibitors. This work was supported by NIEHS grant ES02710, NSF grant DCB-8518697 and the Superfund Basic Reseach Program (Grant P42-ES04699). Josefina Casas was supported by a Fulbright-Spanish Ministry of Education Fellowship. B. Hammock was supported as a Burroughs Wellcome Toxicology Scholar.

PY - 1991

Y1 - 1991

N2 - Epoxide hydrolase (EH) activity in Drosophila melanogaster cell fractions was characterized using juvenile hormone (JH III) and cis-stilbene oxide (CSO) as substrates. A comparison of detergents indicated that 0.3% Lubrol PX was relatively effective for solubilizing EH activity from the 20,000 and 100,000 g pellets. The effect of inhibitors, pH, temperature, salt and organic solvents on EH activity depended on the substrate and cell fraction tested, which suggested there were multiple activities present. For initial purification, polyethylene glycol was useful for precipitating EH activity from the 100,000 g supernatant.

AB - Epoxide hydrolase (EH) activity in Drosophila melanogaster cell fractions was characterized using juvenile hormone (JH III) and cis-stilbene oxide (CSO) as substrates. A comparison of detergents indicated that 0.3% Lubrol PX was relatively effective for solubilizing EH activity from the 20,000 and 100,000 g pellets. The effect of inhibitors, pH, temperature, salt and organic solvents on EH activity depended on the substrate and cell fraction tested, which suggested there were multiple activities present. For initial purification, polyethylene glycol was useful for precipitating EH activity from the 100,000 g supernatant.

KW - Drosophila melanogaster

KW - epoxide hydrolase

KW - juvenile hormone

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U2 - 10.1016/0020-1790(91)90095-V

DO - 10.1016/0020-1790(91)90095-V

M3 - Article

AN - SCOPUS:0001059808

SN - 0020-1790

VL - 21

SP - 887

EP - 894

JO - Insect Biochemistry

JF - Insect Biochemistry

IS - 8

ER -

Epoxide hydrolase activities in Drosophila melanogaster

Abstract

Keywords

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