Inhibition of hepatic mixed function oxidase activity by propyl gallate

Chung S. Yang, Frederick S. Strickhart

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Abstract

Propyl gallate was found to inhibit microsomal benzpyrene hydroxylase activity and demethylase activity with ethylmorphine, aminopyrine or benzphetamine as a substrate. The extent of inhibition with different substrates varied with the age and diet of the animals. The benzpyrene hydroxylase activity of the microsomes of the 3-methylcholanthrene-treated rats was shown to be less susceptible to propyl gallate inhibition. Propyl gallate does not inhibit the NADPH-dependent reduction of cytochrome P-450; therefore, the site of inhibition is not on NADPH-cytochrome c reductase as suggested previously. Propyl gallate interacts with cytochrome P-450 to produce a positive absorption peak around 420 nm, and it may also interfere with the binding of a type I substrate, benzphetamine. It inhibits ethylmorphine demethylation by a noncompetitive mechanism and aminopyrine demethylation by a mixed mechanism. The mode of propyl gallate inhibition and the implications of these observations are discussed.

Original languageEnglish (US)
Pages (from-to)3129-3138
Number of pages10
JournalBiochemical Pharmacology
Volume23
Issue number22
DOIs
StatePublished - Nov 15 1974

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Pharmacology

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