Tolbutamide hydroxylation by hepatic microsomes from Atlantic salmon (Salmo salar L.)

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12520%2F12%3A43883439" target="_blank" >RIV/60076658:12520/12:43883439 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1007/s11033-012-1512-4" target="_blank" >http://dx.doi.org/10.1007/s11033-012-1512-4</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s11033-012-1512-4" target="_blank" >10.1007/s11033-012-1512-4</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Tolbutamide hydroxylation by hepatic microsomes from Atlantic salmon (Salmo salar L.)

Popis výsledku v původním jazyce

Metabolic transformations of two substrates for human cytochrome P450 (CYP450) 2C9, tolbutamide and diclofenac, were investigated in hepatic microsomes from Atlantic salmon (Salmo salar L.). Tolbutamide hydroxylation followed Michaelis-Menten kinetics. Mean apparent Michaelis-Menten constant (K-m) and maximum reaction velocity (V-max) values for 4-hydroxytolbutamide (TBOH) formation were 0.09 +/- A 0.031 mM and 49.5 +/- A 6.03 pmol/min/mg, respectively. Addition of sulfaphenazole, an inhibitor for mammalian CYP2C9, in a range from 1 to 200 mu M decreased formation of TBOH in a concentration-dependent manner, but not to 50%. Neither fluconazole, an inhibitor of human CYP2C9, nor ketoconazole, inhibitor of CYP1A and CYP3A in fish, affected TBOH formation. In contrast ellipticine, an inhibitor of CYP1A in fish inhibited TBOH formation with the IC50 value of 12.1 mu M. The rate of TBOH formation was competitively inhibited by 100 mu M of sesamin in the incubations, but the degree of inhibi

Název v anglickém jazyce

Tolbutamide hydroxylation by hepatic microsomes from Atlantic salmon (Salmo salar L.)

Popis výsledku anglicky

Metabolic transformations of two substrates for human cytochrome P450 (CYP450) 2C9, tolbutamide and diclofenac, were investigated in hepatic microsomes from Atlantic salmon (Salmo salar L.). Tolbutamide hydroxylation followed Michaelis-Menten kinetics. Mean apparent Michaelis-Menten constant (K-m) and maximum reaction velocity (V-max) values for 4-hydroxytolbutamide (TBOH) formation were 0.09 +/- A 0.031 mM and 49.5 +/- A 6.03 pmol/min/mg, respectively. Addition of sulfaphenazole, an inhibitor for mammalian CYP2C9, in a range from 1 to 200 mu M decreased formation of TBOH in a concentration-dependent manner, but not to 50%. Neither fluconazole, an inhibitor of human CYP2C9, nor ketoconazole, inhibitor of CYP1A and CYP3A in fish, affected TBOH formation. In contrast ellipticine, an inhibitor of CYP1A in fish inhibited TBOH formation with the IC50 value of 12.1 mu M. The rate of TBOH formation was competitively inhibited by 100 mu M of sesamin in the incubations, but the degree of inhibi

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2012

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Molecular Biology Reports

ISSN

0301-4851

e-ISSN

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Svazek periodika

39

Číslo periodika v rámci svazku

6

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

7

Strana od-do

6867-6873

Kód UT WoS článku

000303351900054

EID výsledku v databázi Scopus

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