Substrate specificity of human liver cytochrome P-450 debrisoquine 4-hydroxylase probed using immunochemical inhibition and chemical modeling

A significant population of humans (5 to 10%) are phenotypic poor metabolizers of debrisoquine. We have isolated the cytochrome P-450 isozyme from rat liver responsible for this activity and have shown that antibodies raised against the protein are able to inhibit this catalytic activity in human li...

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Veröffentlicht in:	Cancer research (Chicago, Ill.) Ill.), 1985-05, Vol.45 (5), p.2116-2122
Hauptverfasser:	WOLFF, T, DISTLERATH, L. M, WORTHINGTON, M. T, GROOPMAN, J. D, HAMMONS, G. J, KADLUBAR, F. F, PROUGH, R. A, MARTIN, M. V, GUENGERICH, F. P
Format:	Artikel
Sprache:	eng
Schlagworte:	Aflatoxin B1 Aflatoxins - metabolism Biological and medical sciences Carcinogenesis, carcinogens and anticarcinogens Chemical agents Cytochrome P-450 CYP2D6 Cytochrome P-450 Enzyme System - analysis Cytochrome P-450 Enzyme System - immunology Debrisoquin - metabolism Humans Hydroxylation Immunochemistry Liver - enzymology Medical sciences Microsomes, Liver - enzymology Mixed Function Oxygenases - analysis Substrate Specificity Tumors
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