Cumene hydroperoxide-mediated inactivation of cytochrome P450 2B1. Identification of an active site heme-modified peptide

Cumene hydroperoxide (CuOOH)-mediated inactivation of cytochromes P450 (P450) results in the degradation of their prosthetic heme to products that alkylate the apoprotein. Indirect approaches suggest that this alkylation occurs at the active site. in order to identify the specific apoprotein site(s)...

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Veröffentlicht in:	The Journal of biological chemistry 1993-01, Vol.268 (1), p.59-65
Hauptverfasser:	KUNQUAN YAO, FALICK, A. M, PATEL, N, CORREIA, M. A
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Apoenzymes - antagonists & inhibitors Apoenzymes - chemistry Apoenzymes - isolation & purification Benzene Derivatives - pharmacology Binding Sites Biological and medical sciences Chromatography, High Pressure Liquid cumene hydroperoxide Cytochrome P-450 Enzyme Inhibitors Cytochrome P-450 Enzyme System - chemistry Cytochrome P-450 Enzyme System - isolation & purification cytochrome P450 Electrophoresis, Polyacrylamide Gel endoplasmic reticulum Fundamental and applied biological sciences. Psychology Heme - metabolism Hemoproteins inactivation Male mechanisms Metalloproteins Microsomes, Liver - enzymology Molecular Sequence Data Molecular Weight Peptide Fragments - isolation & purification Proteins Rats Rats, Wistar Spectrophotometry
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