Denaturation of cytochrome P-450 by cyclophosphamide metabolites
| Autor: | A.J. Marinello, R.F. Struck, Hira L. Gurtoo, Brajeswar Paul |
|---|---|
| Rok vydání: | 1978 |
| Předmět: |
Oxygenase
Protein Denaturation Cytochrome Metabolite Biophysics Biochemistry chemistry.chemical_compound Cytochrome P-450 Enzyme System Animals Denaturation (biochemistry) Ifosfamide Acrolein Molecular Biology Cyclophosphamide Biotransformation Aldehydes biology Cell Biology Phosphoramide Mustard Rats chemistry biology.protein Microsome Microsomes Liver Phosphoramide Mustards Cysteine |
| Zdroj: | Biochemical and biophysical research communications. 83(4) |
| ISSN: | 0006-291X |
| Popis: | Cyclophosphamide (CP) metabolites, acrolein and 4-hydroxy-CP, were found to denature rat liver microsomal cytochrome P-450, whereas another metabolite, phosphoramide mustard, CP per se or its analog Ifosfamide had no effect. The denaturation produced by CP metabolites could be blocked by cysteine, suggesting an interaction between CP metabolite(s) and sulfhydryl groups in cysteine and probably in cytochrome P-450. These studies might explain the biochemical basis of the specific depression of various microsomal mixed function oxygenase activities produced by high doses of CP. |
| Databáze: | OpenAIRE |
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