Kinetics of ethylmorphine N-demethylase at low substrate concentrations and its implications concerning the role of the stimulation of NADPH-cytochrome P-450 reductase activity in mixed-function oxidase activity

John A. Thompson; Jordan L. Holtzman

doi:10.1016/0006-2952(77)90349-5

Kinetics of ethylmorphine N-demethylase at low substrate concentrations and its implications concerning the role of the stimulation of NADPH-cytochrome P-450 reductase activity in mixed-function oxidase activity

John A. Thompson
, Jordan L. Holtzman

University of Minnesota Twin Cities

Research output: Contribution to journal › Article › peer-review

8 Scopus citations

Abstract

The 1:1 stoichiometry observed in previous studies between the stimulation of NADPH-cytochrome P-450 reductase activity and ethylmorphine N-demethylase would imply that the stimulation of reduction is the rate-limiting process in the N-demethylation. In the present study, we have found that double reciprocal plots of the N-demethylase activity of hepatic microsomes from male and female rats is linear for ethylmorphine concentrations from 2.5 μM to 2mM. Kinetic analysis suggests that these linear plots are not compatible with the stimulation of the reductase being the rate-limiting process.

Original language	English (US)
Pages (from-to)	1803-1807
Number of pages	5
Journal	Biochemical Pharmacology
Volume	26
Issue number	19
DOIs	https://doi.org/10.1016/0006-2952(77)90349-5
State	Published - Oct 1 1977

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Kinetics of ethylmorphine N-demethylase at low substrate concentrations and its implications concerning the role of the stimulation of NADPH-cytochrome P-450 reductase activity in mixed-function oxidase activity. / Thompson, John A.; Holtzman, Jordan L.
In: Biochemical Pharmacology, Vol. 26, No. 19, 01.10.1977, p. 1803-1807.

Research output: Contribution to journal › Article › peer-review

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abstract = "The 1:1 stoichiometry observed in previous studies between the stimulation of NADPH-cytochrome P-450 reductase activity and ethylmorphine N-demethylase would imply that the stimulation of reduction is the rate-limiting process in the N-demethylation. In the present study, we have found that double reciprocal plots of the N-demethylase activity of hepatic microsomes from male and female rats is linear for ethylmorphine concentrations from 2.5 μM to 2mM. Kinetic analysis suggests that these linear plots are not compatible with the stimulation of the reductase being the rate-limiting process.",

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N2 - The 1:1 stoichiometry observed in previous studies between the stimulation of NADPH-cytochrome P-450 reductase activity and ethylmorphine N-demethylase would imply that the stimulation of reduction is the rate-limiting process in the N-demethylation. In the present study, we have found that double reciprocal plots of the N-demethylase activity of hepatic microsomes from male and female rats is linear for ethylmorphine concentrations from 2.5 μM to 2mM. Kinetic analysis suggests that these linear plots are not compatible with the stimulation of the reductase being the rate-limiting process.

AB - The 1:1 stoichiometry observed in previous studies between the stimulation of NADPH-cytochrome P-450 reductase activity and ethylmorphine N-demethylase would imply that the stimulation of reduction is the rate-limiting process in the N-demethylation. In the present study, we have found that double reciprocal plots of the N-demethylase activity of hepatic microsomes from male and female rats is linear for ethylmorphine concentrations from 2.5 μM to 2mM. Kinetic analysis suggests that these linear plots are not compatible with the stimulation of the reductase being the rate-limiting process.

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Kinetics of ethylmorphine N-demethylase at low substrate concentrations and its implications concerning the role of the stimulation of NADPH-cytochrome P-450 reductase activity in mixed-function oxidase activity

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