Fluorescein Isothiocyanate Specifically Modifies Lysine 338 of Cytochrome P-450scc and Inhibits Adrenodoxin Binding
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference21 articles.
1. Modification of cytochrome P-450 with fluorescein isothiocyanate
2. Selective chemical modification of a functionally linked lysine in cytochrome P-450 LM2
3. Cross-linking studies of adrenocortical cytochrome P-450scc. Evidence for a covalent complex with adrenodoxin and localization of the adrenodoxin-binding domain
4. Primary structure of the cholesterol side-chain cleavage cytochrome P-450 from bovine adrenocortical mitochondria and some aspects of its functioning on a structural level
5. Experimental Evidence for a Hydrophobic Active Center of Glutamic-Aspartic Transaminase. Specific Interaction of Holoenzyme and Apoenzyme with Two Fluorescein Derivatives
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