Studies on the identity of the heme-binding cysteinyl residue in rabbit liver microsomal cytochrome P-450 isozyme 2
- 1 April 1985
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 128 (1), 82-89
- https://doi.org/10.1016/0006-291x(85)91647-x
Abstract
No abstract availableThis publication has 37 references indexed in Scilit:
- Structural analysis of the cysteine-containing peptides from the major 3-methylcholanthrene-induced isozyme of cytochrome P-450 (P-450c) in rat liver microsomesBiochemistry, 1984
- Nucleotide sequence of a full-length cDNA coding for 3-methylcholanthrene-induced rat liver cytochrome P-450MCNucleic Acids Research, 1984
- Mouse cytochrome P3-450: complete cDNA and amino acid sequenceNucleic Acids Research, 1984
- Steroid 21-hydroxylase (cytochrome P-450) from porcine adrenocortical microsomes: microsequence analysis of cysteine-containing peptidesBiochemistry, 1983
- Resonance Raman detection of an iron-sulfur bond in cytochrome P 450camJournal of the American Chemical Society, 1982
- Simple, rapid, and highly efficient separation of amino acid phenylthiohydantoins by reversed-phase high-performance liquid chromatographyAnalytical Biochemistry, 1982
- The primary structure of the monoxygenase cytochrome P450CAMBiochemical and Biophysical Research Communications, 1982
- Oxygen Activation by Cytochrome P-4501Annual Review of Biochemistry, 1980
- Determination of sulfhydryl groups with 2,2′- or 4,4′-dithiodipyridineArchives of Biochemistry and Biophysics, 1967
- Tissue sulfhydryl groupsArchives of Biochemistry and Biophysics, 1959