The Inactivation of Cytochrome P450 3A5 by 17α-Ethynylestradiol Is Cytochromeb5-Dependent: Metabolic Activation of the Ethynyl Moiety Leads to the Formation of Glutathione Conjugates, a Heme Adduct, and Covalent Binding to the Apoprotein-Reference-Cited by-同舟云学术

The Inactivation of Cytochrome P450 3A5 by 17α-Ethynylestradiol Is Cytochromeb5-Dependent: Metabolic Activation of the Ethynyl Moiety Leads to the Formation of Glutathione Conjugates, a Heme Adduct, and Covalent Binding to the Apoprotein

Published:2007-01-24 Issue:1 Volume:321 Page:276-287
ISSN:0022-3565
Container-title:Journal of Pharmacology and Experimental Therapeutics
language:en
Short-container-title:J Pharmacol Exp Ther

Author:

Lin Hsia-lien,Hollenberg Paul F.

Publisher

American Society for Pharmacology & Experimental Therapeutics (ASPET)

Subject

Pharmacology,Molecular Medicine

Reference39 articles.

1. Mass spectrometry in the analysis of glutathione conjugates

2. Mechanism-Based Inactivation of Cytochromes P450 2E1 and 2E1 T303A by tert-Butyl Acetylenes: Characterization of Reactive Intermediate Adducts to the Heme and Apoprotein

3. Studies on the Metabolism of Ethynylestradiolin vitroandin vivo: The Significance of 2-Hydroxylation and the Formation of Polar Products

4. The catalytic site of rat hepatic lauric acid omega-hydroxylase. Protein versus prosthetic heme alkylation in the omega-hydroxylation of acetylenic fatty acids.

5. Determinants of protein modification versus heme alkylation: inactivation of cytochrome P450 1A1 by 1-ethynylpyrene and phenylacetylene

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