Identification of the Ah receptor in selected mammalian species and induction of aryl hydrocarbon hydroxylase

M. S. Denison, C. F. Wilkinson

Research output: Contribution to journalArticle

52 Citations (Scopus)

Abstract

The Ah receptor protein, important in the mechanism of induction of aryl hydrocarbon hydroxylase activity, has been identified and partially characterized in hepatic cytosolic preparations from rat, BALB/c mouse, gerbil, hamster, rabbit, ferret and guinea-pig by means of sucrose density centrifugation analysis and hydroxyapatite binding assays. Using 2,3,7,8-tetrachloro[3H]dibenzo-p-dioxin (TCDD) as the ligand, total specific binding capacities ranged over 74-691 fmol [3H]TCDD/mg cytosolic protein and apparent dissociation constants ranged over 0.30-7.8 nM. There was no quantitative correlation between the concentration of cytosolic Ah receptors and the 3-methylcholanthrene-mediated induction of aryl hydrocarbon hydroxylase activity in the species studied. Competitive binding studies with a series of monohydroxylated benzo[a]pyrene derivatives suggested the importance of electronic character in their ability to bind to the Ah receptor and to compete with TCDD for specific binding sites on the receptor.

Original languageEnglish (US)
Pages (from-to)429-435
Number of pages7
JournalEuropean Journal of Biochemistry
Volume147
Issue number2
StatePublished - 1985
Externally publishedYes

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Aryl Hydrocarbon Hydroxylases
Methylcholanthrene
Centrifugation
Benzo(a)pyrene
Durapatite
Sucrose
Rats
Assays
Ferrets
Proteins
Competitive Binding
Gerbillinae
Binding Sites
Ligands
Derivatives
Cricetinae
Guinea Pigs
Rabbits
Liver
Polychlorinated Dibenzodioxins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Identification of the Ah receptor in selected mammalian species and induction of aryl hydrocarbon hydroxylase. / Denison, M. S.; Wilkinson, C. F.

In: European Journal of Biochemistry, Vol. 147, No. 2, 1985, p. 429-435.

Research output: Contribution to journalArticle

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