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Abstract

Mephenytoin metabolism in vitro by human liver.

M Jurima, T Inaba and W Kalow
Drug Metabolism and Disposition March 1985, 13 (2) 151-155;
M Jurima
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T Inaba
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W Kalow
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Abstract

Human liver was used in investigations of mephenytoin p-hydroxylase, the enzyme presumably responsible for the genetic polymorphism in mephenytoin metabolism. A gas chromatographic assay method was developed to measure p-hydroxylation and N-demethylation which is the other major metabolic pathway. Both reactions were localized in the microsomal fraction and required NADPH. Inhibition of p-hydroxylation by CO, SKF 525-A, and metyrapone was demonstrated. It was concluded that a form of cytochrome P-450 catalyzes the reaction. The velocity of N-demethylation in human liver did not show saturation even at 500 microM substrate concentration. The p-hydroxylation, however, followed Michaelis-Menten kinetics. The Km, determined in five different livers, ranged from 59 to 143 microM. The linearity in Eadie-Hofstee plots was consistent with the involvement of a single catalytic site.

 

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Drug Metabolism and Disposition
Vol. 13, Issue 2
1 Mar 1985
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Abstract

Mephenytoin metabolism in vitro by human liver.

M Jurima, T Inaba and W Kalow
Drug Metabolism and Disposition March 1, 1985, 13 (2) 151-155;

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Abstract

Mephenytoin metabolism in vitro by human liver.

M Jurima, T Inaba and W Kalow
Drug Metabolism and Disposition March 1, 1985, 13 (2) 151-155;
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