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Xenobiotica
the fate of foreign compounds in biological systems
Volume 11, 1981 - Issue 11
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Research Article

Xenobiotic biotransformation in wild birds: Activity, induction, characterization and comparison with rat and mouse microsomal enzymes

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Pages 785-793 | Received 13 Jun 1981, Published online: 22 Sep 2008
 

Abstract

1. Benzo[a]pyrene hydroxylase, aminopyrine demethylase and glutathione S-trans-ferase activities in hepatic and extrahepatic tissues of five wild birds, rat and mouse were compared.

2. Hepatic benzo[a]pyrene hydroxylase of wild pigeon was at least three times higher than that of rat or mouse. Hepatic aminopyrine demethylase and GSH S-transferase activities of wild birds were lower than those of rodents.

3. Renal GSH S-transferase of wild birds was 2-3 times more than in rat and mouse.

4. Avian benzo[a]pyrene hydroxylase activity of hepatic and renal tissue was linear up to 3.0 mg enzyme protein with pH optima of 7.4 and 7.2, at 42°C Apparent Km values were 11.76 and 3.33 μM respectively.

5. Hepatic enzyme activity was induced four-fold by 3-methylcholanthrene and about two-fold by phenobarbitone administration.

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