Biochemical characterization of a variant form of cytosolic epoxide hydrolase induced by parental exposure to N-ethyl-N-nitrosourea |
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| Institution: | 1. Division of Endocrinology and Metabolism, Department of Internal Medicine, College of Medicine, Hallym University, Seoul, South Korea;2. Division of Endocrinology and Metabolism, Department of Internal Medicine, College of Medicine, Korea University, Seoul, South Korea;1. Department of Biomechanics, College of Education, Biomechanics Research Building 6160 University Drive South Omaha, University of Nebraska at Omaha, Omaha, NE, USA;2. Department of Biomechanics, the University of Nebraska at Omaha, Omaha, NE, USA;3. Department of Health and Kinesiology, the University of Nebraska at Omaha, Omaha, NE, USA;4. Department of Surgery, University of Nebraska Medical Center, Omaha, NE, USA;5. Department of Surgery and Research Service, Omaha VA Medical Center, Omaha, NE, USA;6. Department of Health Promotion, College of Public Health, University of Nebraska Medical Center, Omaha, USA |
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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. |
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