Studies on the identity of the heme-binding cysteinyl residue in rabbit liver microsomal cytochrome P-450 isozyme 2
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference33 articles.
1. The complete amino acid sequence of rabbit phenobarbital-induced liver microsomal cytochrome P-450.
2. Purified liver microsomal cytochrome P-450. Separation and characterization of multiple forms.
3. Properties of electrophoretically homogeneous phenobarbital-inducible and beta-naphthoflavone-inducible forms of liver microsomal cytochrome P-450
4. Oxygen Activation by Cytochrome P-4501
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3. Comparative Study on the Bioactivation Mechanisms and Cytotoxicity of Te-Phenyl-l-tellurocysteine, Se-Phenyl-l-selenocysteine, and S-Phenyl-l-cysteine;Chemical Research in Toxicology;2002-12-01
4. Heme Oxygenase-2 Interaction with Metalloporphyrins: Function of Heme Regulatory Motifs;Antioxidants & Redox Signaling;2001-08
5. Activation of Microsomal Glutathione S-Transferase and Inhibition of Cytochrome P450 1A1 Activity as a Model System for Detecting Protein Alkylation by Thiourea-Containing Compounds in Rat Liver Microsomes;Chemical Research in Toxicology;1999-04-07
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