Binding of pyridine derivatives to cytochrome P-450
β Scribed by Jerry L. Born; David Vaughn
- Publisher
- John Wiley and Sons
- Year
- 1977
- Tongue
- English
- Weight
- 256 KB
- Volume
- 66
- Category
- Article
- ISSN
- 0022-3549
No coin nor oath required. For personal study only.
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The oxidation of uroporphyrinogen, an intermediate of the heme biosynthetic pathway, by methylcholanthrene-inducible isozyme(s) of cytochrome P-450 has been proposed to play a role in the development of chemically induced uroporphyria. Prior work from this laboratory [lo] indicated that although add
## Abstract Cytochrome P450s (CYPs) are important hemeβcontaining proteins that play important roles in the metabolism of xenobiotics and endogenous compounds. The oxidative metabolisms of drugs, environmental chemicals, hormones, and fatty acids by CYP enzymes are critical pathways aiding in their
Investigation of the difference absorption spectrum has been a common method for studying many aspects of hemoproteins such as cytochrome P450. The difference spectrophotometric technique, as applied in studies on binding of substrates to cytochrome P450, has resulted in certain mathematical artifac