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Differences in the biochemical properties of aldrin epoxidase, a cytochrome P-450-dependent monooxygenase, in various tissues.

Abstract：

:Aldrin epoxidase, a cytochrome P-450-dependent monooxygenase, was studied in the lung and kidney of male rats. The sensitivity of the liver enzyme activity to different chemicals in vitro was influenced by the treatment of the animals with phenobarbital or methylcholanthrene. These results confirm that more than one form of cytochrome P-450 supports aldrin epoxidase in the liver. The lung and kidney aldrin epoxidase activity was not modified by the administration of chemical inducers to the rats. In vitro, the lung and kidney aldrin epoxidase activities were activated by tetrahydrofurane and progesterone, respectively. The results obtained from the lung and kidney indicate that one single species of cytochrome P-450, associated with aldrin epoxidase, exists in these organs, but it may be a different type, or regulated in a different manner in these tissues.

journal_name

Biochem Pharmacol

journal_title

Biochemical pharmacology

authors

Van Cantfort J,Léonard-Poma M,Sèle-Doyen J,Gielen JE

doi

10.1016/0006-2952(83)90078-3

subject

Has Abstract

pub_date

1983-09-15 00:00:00

pages

2697-702

issue

18

eissn

0006-2952

issn

1873-2968

pii

0006-2952(83)90078-3

journal_volume

32

pub_type

杂志文章

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