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HERO ID
5126592
Reference Type
Journal Article
Title
Epoxide hydrase activity in liver nuclei: hydration of benzo[a]pyrene-4,5-oxide and styrene oxide
Author(s)
Bornstein, WA; Chuang, H; Bresnick, E; Mukhtar, H; Bend, JR
Year
1978
Is Peer Reviewed?
Yes
Journal
Chemico-Biological Interactions
ISSN:
0009-2797
EISSN:
1872-7786
Volume
21
Issue
2-3
Page Numbers
343-346
Language
English
PMID
679405
DOI
10.1016/0009-2797(78)90032-7
Web of Science Id
WOS:A1978FN07100018
URL
https://www.scopus.com/inward/record.uri?eid=2-s2.0-0017852146&doi=10.1016%2f0009-2797%2878%2990032-7&partnerID=40&md5=9e2a6e87491f2d9d51e0e6d37ce3c6b8
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Abstract
The effects of benzo(a)pyrene-4,5-oxide (37574473) (BP-4,5-oxide) and styrene-oxide (96093) on epoxide hydrase activity in liver nuclei were studied. Purified liver nuclei from Sprague-Dawley-rats were incubated with the test substances by high pressure liquid chromatography (HPLC) assay and by radioactive assay. In some tests, an oxide of a polycyclic hydrocarbon was used as a substrate. Trans diol formation was determined as a function of time and nuclear protein. In the HPLC assay using BP-4,5-oxide, enzyme activity was directly proportional to nuclear protein up to a concentration of 10 milligrams (mg) and up to 20 minutes of incubation. In the radioactive assay, linear relationships occurred for styrene-oxide up to 3mg nuclear protein and 10 minutes of incubation and for BP-4,5-oxide up to 1mg protein and 15 minutes of incubation. Epoxide hydrase activity of purified liver nuclei by either assay method was 0.33 to 0.35 nanomoles per minute (nmol/min) per mg protein with BP-4,5-oxide and 0.41nmol/min/mg protein with styrene-oxide. The authors conclude that the liver nucleus not only is a prime target for the action of polycyclic hydrocarbons but also may be the mechanism for metabolic activation of these substances for mutagenesis, teratogenesis or carcinogenesis.
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