Identification of a human liver cytochrome P-450 exhibiting catalytic and immunochemical similarities to cytochrome P-450 3a of rabbit liver

Judy Raucy; Peter Fernandes; Martin Black; Shin L. Yang; Dennis R. Koop

doi:10.1016/0006-2952(87)90203-6

Identification of a human liver cytochrome P-450 exhibiting catalytic and immunochemical similarities to cytochrome P-450 3a of rabbit liver

Judy Raucy, Peter Fernandes, Martin Black, Shin L. Yang, Dennis R. Koop

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Abstract

Immunoblot analysis of liver microsomes from nine patients demonstrated that each contained a cytochrome P-450 that reacted with an antibody directed against the ethanol-inducible rabbit liver cytochrome, P-450 3a. Two of the liver specimens exhibited high concentrations of the immunoreactive protein, high rates of aniline hydroxylation and N-nitrosodimethylamine demethylation, and extensive inhibition of activity in the presence of antibody to P-450 3a. One other liver specimen exhibited a very low rate of aniline hydroxylation with significantly less antibody inhibition. The variability witnessed was independent of the alcohol history of the individual patients, suggesting that the human cytochrome may be under some other environmental, dietary or genetic regulation. Its inducibility by ethanol was not directly studied in this investigation. However, we conclude that there is a cytochrome P-450 present in human liver which is immunochemically and catalytically similar to the ethanol-inducible P-450 of rabbit liver.

Original language	English (US)
Pages (from-to)	2921-2926
Number of pages	6
Journal	Biochemical Pharmacology
Volume	36
Issue number	18
DOIs	https://doi.org/10.1016/0006-2952(87)90203-6
State	Published - Sep 15 1987
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Pharmacology

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title = "Identification of a human liver cytochrome P-450 exhibiting catalytic and immunochemical similarities to cytochrome P-450 3a of rabbit liver",

abstract = "Immunoblot analysis of liver microsomes from nine patients demonstrated that each contained a cytochrome P-450 that reacted with an antibody directed against the ethanol-inducible rabbit liver cytochrome, P-450 3a. Two of the liver specimens exhibited high concentrations of the immunoreactive protein, high rates of aniline hydroxylation and N-nitrosodimethylamine demethylation, and extensive inhibition of activity in the presence of antibody to P-450 3a. One other liver specimen exhibited a very low rate of aniline hydroxylation with significantly less antibody inhibition. The variability witnessed was independent of the alcohol history of the individual patients, suggesting that the human cytochrome may be under some other environmental, dietary or genetic regulation. Its inducibility by ethanol was not directly studied in this investigation. However, we conclude that there is a cytochrome P-450 present in human liver which is immunochemically and catalytically similar to the ethanol-inducible P-450 of rabbit liver.",

author = "Judy Raucy and Peter Fernandes and Martin Black and Yang, {Shin L.} and Koop, {Dennis R.}",

note = "Funding Information: * This study was supported by Smith, Kline Br French Laboratories and the Benjamin Franklin Partnership Award. t To whom correspondence should be addressed!",

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doi = "10.1016/0006-2952(87)90203-6",

language = "English (US)",

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T1 - Identification of a human liver cytochrome P-450 exhibiting catalytic and immunochemical similarities to cytochrome P-450 3a of rabbit liver

AU - Raucy, Judy

AU - Fernandes, Peter

AU - Black, Martin

AU - Yang, Shin L.

AU - Koop, Dennis R.

N1 - Funding Information: * This study was supported by Smith, Kline Br French Laboratories and the Benjamin Franklin Partnership Award. t To whom correspondence should be addressed!

PY - 1987/9/15

Y1 - 1987/9/15

N2 - Immunoblot analysis of liver microsomes from nine patients demonstrated that each contained a cytochrome P-450 that reacted with an antibody directed against the ethanol-inducible rabbit liver cytochrome, P-450 3a. Two of the liver specimens exhibited high concentrations of the immunoreactive protein, high rates of aniline hydroxylation and N-nitrosodimethylamine demethylation, and extensive inhibition of activity in the presence of antibody to P-450 3a. One other liver specimen exhibited a very low rate of aniline hydroxylation with significantly less antibody inhibition. The variability witnessed was independent of the alcohol history of the individual patients, suggesting that the human cytochrome may be under some other environmental, dietary or genetic regulation. Its inducibility by ethanol was not directly studied in this investigation. However, we conclude that there is a cytochrome P-450 present in human liver which is immunochemically and catalytically similar to the ethanol-inducible P-450 of rabbit liver.

AB - Immunoblot analysis of liver microsomes from nine patients demonstrated that each contained a cytochrome P-450 that reacted with an antibody directed against the ethanol-inducible rabbit liver cytochrome, P-450 3a. Two of the liver specimens exhibited high concentrations of the immunoreactive protein, high rates of aniline hydroxylation and N-nitrosodimethylamine demethylation, and extensive inhibition of activity in the presence of antibody to P-450 3a. One other liver specimen exhibited a very low rate of aniline hydroxylation with significantly less antibody inhibition. The variability witnessed was independent of the alcohol history of the individual patients, suggesting that the human cytochrome may be under some other environmental, dietary or genetic regulation. Its inducibility by ethanol was not directly studied in this investigation. However, we conclude that there is a cytochrome P-450 present in human liver which is immunochemically and catalytically similar to the ethanol-inducible P-450 of rabbit liver.

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Identification of a human liver cytochrome P-450 exhibiting catalytic and immunochemical similarities to cytochrome P-450 3a of rabbit liver

Abstract

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