Elsevier

Biochemical Pharmacology

Volume 36, Issue 14, 15 July 1987, Pages 2325-2330
Biochemical Pharmacology

In vitro inhibition of phenolsulphotransferase by food and drink constituents

https://doi.org/10.1016/0006-2952(87)90598-3Get rights and content

Abstract

Several natural and synthetic food and drink constituents were tested in vitro for their inhibitory actions on phenolsulphotransferase P and M (PST P, PST M) and monoamine oxidase A and B (MAO A, MAO B). Cyanidin 3-rutinoside, a simple anthocyanin, (+)-catechin, a flavanol, and carmoisine, a synthetic food colorant, were found to be particularly potent, reversible inhibitors of PST P. All inhibited this enzyme by 100% at a concentration of 5 μM. and had an IC50 in the μM range. The effects of these compounds on PST M and MAO A and B were less pronounced. There was a considerable difference in the inhibitory ability of different purified anthocyanins but all were selective for PST P. Several other phenolic food colorants were also found to be specific inhibitors of PST P, though less potent in their actions. Tartrazine, a non-phenolic food colorant, had little effect. The phenolic extracts from two red wines were also found selectively to inhibit PST P in vitro, suggesting that it is within this fraction that these inhibitors are to be found.

PST is an important enzyme involved in the inactivation of a wide range of exogenous and endogenous phenols. If such a degree of inhibition were to occur in vivo, potentially toxic concentrations of some phenolic substrates might result.

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