EsturgeonV1, Istex, Corpus, bibRecord, 000810

Characterization of xenobiotic metabolizing enzymes in sturgeon ( Acipenser baeri )

Identifieur interne : 000810 ( Istex/Corpus ); précédent : 000809; suivant : 000811

Characterization of xenobiotic metabolizing enzymes in sturgeon ( Acipenser baeri )

Auteurs : E. F. Perdu-Durand ; J. P. Cravedi

Source :

Comparative Biochemistry and Physiology, Part B: Biochemistry and Molecular Biology [ 0305-0491 ] ; 1989.

RBID : ISTEX:8AC654402F5A07507E1494439A0D4D22218D878F

Abstract

1.1. Cytochrome P-450, NADPH-cytochrome c reductase, benzo(a)-pyrene hydroxylase (AHH), 7-ethoxycoumarin-O-deethylase (7-ECOD), epoxide hydrolase (EH), UDP-glucuronyltransferase (UDPGT) and glutathione S-transferase (GSHST) activities in sturgeon (Acipenser baeri) have been measured and partially characterized.2.2. Cytochrome P-450-dependent monoxygenase (MO), EH, and conjugation reactions were detected in liver and to a lesser extent in kidney and gills.3.3. Hepatic enzyme activities in the sturgeon were equally high or higher than in rainbow trout liver, with the exception of UDPGT whose activity was 14% of that in trout liver.4.4. The MO and EH activities displayed the expected pH maxima of 7.5, whereas transferases were relatively independent of the pH in the 6.5–7.5 range.5.5. The temperature optima for MO and EH were close to those reported in other fish species, whereas for conjugation reactions the temperature optima were 45 and 60°C for GSHST and UDPGT respectively.

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https://api.istex.fr/document/8AC654402F5A07507E1494439A0D4D22218D878F/fulltext/pdf

DOI: 10.1016/0305-0491(89)90067-9

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ISTEX:8AC654402F5A07507E1494439A0D4D22218D878F

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<head><ce:title>Characterization of xenobiotic metabolizing enzymes in sturgeon (<ce:italic>Acipenser baeri</ce:italic>
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<ce:para>1. Cytochrome P-450, NADPH-cytochrome c reductase, benzo(a)-pyrene hydroxylase (AHH), 7-ethoxycoumarin-O-deethylase (7-ECOD), epoxide hydrolase (EH), UDP-glucuronyltransferase (UDPGT) and glutathione S-transferase (GSHST) activities in sturgeon (<ce:italic>Acipenser baeri</ce:italic>
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<ce:list-item><ce:label>2.</ce:label>
<ce:para>2. Cytochrome P-450-dependent monoxygenase (MO), EH, and conjugation reactions were detected in liver and to a lesser extent in kidney and gills.</ce:para>
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<ce:para>3. Hepatic enzyme activities in the sturgeon were equally high or higher than in rainbow trout liver, with the exception of UDPGT whose activity was 14% of that in trout liver.</ce:para>
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<ce:para>4. The MO and EH activities displayed the expected pH maxima of 7.5, whereas transferases were relatively independent of the pH in the 6.5–7.5 range.</ce:para>
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<ce:list-item><ce:label>5.</ce:label>
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Characterization of xenobiotic metabolizing enzymes in sturgeon ( Acipenser baeri )

Characterization of xenobiotic metabolizing enzymes in sturgeon ( Acipenser baeri )

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