Biochemical characterization of a variant form of cytosolic epoxide hydrolase induced by parental exposure to N-ethyl-N-nitrosourea

Jaffar Nourooz-Zadeh; Bruce S. Winder; Eric C. Dietze; Carol S. Giometti; Sandra L. Tollaksen; Bruce D. Hammock

doi:10.1016/0742-8413(92)90253-4

Biochemical characterization of a variant form of cytosolic epoxide hydrolase induced by parental exposure to N-ethyl-N-nitrosourea

Jaffar Nourooz-Zadeh, Bruce S. Winder, Eric C. Dietze, Carol S. Giometti, Sandra L. Tollaksen, Bruce D. Hammock

Entomology

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Abstract

1. ENU4 mice express a protein variant originally detected in a CBF1 mouse sired by a C57BL/6 mouse exposed to N-ethyl-N-nitrosourea. It appears to be an isolelectric point variant of cytosolic epoxide hydrolase. Affinity purified cytosolic epoxide hydrolase from ENU4 mice has a pI of approximately 5.1 compared to 5.6 in other mouse strains. 2. Clofibrate induced cytosolic epoxide hydrolase to similar levels in five strains of mice. However, CBF1 and ENU4 mice were more sensitive to the induction of palmitoyl CoA oxidase activity. 3. Except for isoelectric point, the physico- and immunochemical properties of cytosolic epoxide hydrolase from ENU4 mice were similar to those of the other mouse strains. Substrate specificities for five of six substrates tested were also similar.

Original language	English (US)
Pages (from-to)	207-214
Number of pages	8
Journal	Comparative Biochemistry and Physiology. Part C, Comparative
Volume	103
Issue number	1
DOIs	https://doi.org/10.1016/0742-8413(92)90253-4
State	Published - 1992

ASJC Scopus subject areas

Pharmacology
Immunology

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Biochemical characterization of a variant form of cytosolic epoxide hydrolase induced by parental exposure to N-ethyl-N-nitrosourea. / Nourooz-Zadeh, Jaffar; Winder, Bruce S.; Dietze, Eric C.; Giometti, Carol S.; Tollaksen, Sandra L.; Hammock, Bruce D.

In: Comparative Biochemistry and Physiology. Part C, Comparative, Vol. 103, No. 1, 1992, p. 207-214.

Research output: Contribution to journal › Article › peer-review

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title = "Biochemical characterization of a variant form of cytosolic epoxide hydrolase induced by parental exposure to N-ethyl-N-nitrosourea",

abstract = "1. ENU4 mice express a protein variant originally detected in a CBF1 mouse sired by a C57BL/6 mouse exposed to N-ethyl-N-nitrosourea. It appears to be an isolelectric point variant of cytosolic epoxide hydrolase. Affinity purified cytosolic epoxide hydrolase from ENU4 mice has a pI of approximately 5.1 compared to 5.6 in other mouse strains. 2. Clofibrate induced cytosolic epoxide hydrolase to similar levels in five strains of mice. However, CBF1 and ENU4 mice were more sensitive to the induction of palmitoyl CoA oxidase activity. 3. Except for isoelectric point, the physico- and immunochemical properties of cytosolic epoxide hydrolase from ENU4 mice were similar to those of the other mouse strains. Substrate specificities for five of six substrates tested were also similar.",

author = "Jaffar Nourooz-Zadeh and Winder, {Bruce S.} and Dietze, {Eric C.} and Giometti, {Carol S.} and Tollaksen, {Sandra L.} and Hammock, {Bruce D.}",

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doi = "10.1016/0742-8413(92)90253-4",

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AU - Nourooz-Zadeh, Jaffar

AU - Winder, Bruce S.

AU - Dietze, Eric C.

AU - Giometti, Carol S.

AU - Tollaksen, Sandra L.

AU - Hammock, Bruce D.

PY - 1992

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N2 - 1. ENU4 mice express a protein variant originally detected in a CBF1 mouse sired by a C57BL/6 mouse exposed to N-ethyl-N-nitrosourea. It appears to be an isolelectric point variant of cytosolic epoxide hydrolase. Affinity purified cytosolic epoxide hydrolase from ENU4 mice has a pI of approximately 5.1 compared to 5.6 in other mouse strains. 2. Clofibrate induced cytosolic epoxide hydrolase to similar levels in five strains of mice. However, CBF1 and ENU4 mice were more sensitive to the induction of palmitoyl CoA oxidase activity. 3. Except for isoelectric point, the physico- and immunochemical properties of cytosolic epoxide hydrolase from ENU4 mice were similar to those of the other mouse strains. Substrate specificities for five of six substrates tested were also similar.

AB - 1. ENU4 mice express a protein variant originally detected in a CBF1 mouse sired by a C57BL/6 mouse exposed to N-ethyl-N-nitrosourea. It appears to be an isolelectric point variant of cytosolic epoxide hydrolase. Affinity purified cytosolic epoxide hydrolase from ENU4 mice has a pI of approximately 5.1 compared to 5.6 in other mouse strains. 2. Clofibrate induced cytosolic epoxide hydrolase to similar levels in five strains of mice. However, CBF1 and ENU4 mice were more sensitive to the induction of palmitoyl CoA oxidase activity. 3. Except for isoelectric point, the physico- and immunochemical properties of cytosolic epoxide hydrolase from ENU4 mice were similar to those of the other mouse strains. Substrate specificities for five of six substrates tested were also similar.

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Biochemical characterization of a variant form of cytosolic epoxide hydrolase induced by parental exposure to N-ethyl-N-nitrosourea

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