Effect of detergents on the N-and ring-hydroxylation of 2-acetamidofluorene by hamster liver microsomal preparations
Autor: | E N Dwyer, Prabhakar D. Lotlikar |
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Rok vydání: | 1976 |
Předmět: |
Male
Cytochrome Detergents Hamster Reductase In Vitro Techniques Hydroxylation Biochemistry chemistry.chemical_compound Animals Molecular Biology Fluorenes Chromatography biology Cell Biology 2-Acetylaminofluorene Stimulation Chemical 2-Acetamidofluorene chemistry Solubilization Microsome biology.protein Microsomes Liver Research Article |
Zdroj: | The Biochemical journal. 160(3) |
ISSN: | 0264-6021 |
Popis: | Effects of detergents such as cholate, deoxycholate and Triton X-100 were studied on N-and ring-hydroxylation of 2-acetamidofluorene by reconstituted and unresolved microsomal systems from livers of hamsters pretreated with 3-methylcholanthrene. Triton X-100 (2.5 mg/nmol of cytochrome P-448) inhibited N-and ring-hydroxylation by wholemicrosomal preparations by 40 and 90% respectively Deoxycholate at the same concentration inhibited both hydroxylations completely, whereas cholate inhibited N-and ring-hydroxylation by 40 and 50% respectively. In reconstitution studies, the presence of Triton X-100(0.5-1.0mg/nmol of cytochrome P-448) along with unsolubilized cytochrome P-448 fraction and solubilized reductase fraction increased N-hydroxylation to an appreciable extent compared with ring-hydroxylation. Both cholate and deoxycholate at 0.5-1.0 mg concentrations had a greater stimulatory effect on ring-than on N-hydroxylation activity in such a reconstituted system. |
Databáze: | OpenAIRE |
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