Abstract

Triethyltin bromide was found to be a selective inhibitor of red cell hexokinase. When intact red cell suspensions were exposed to the reagent (0.025–0.5 mM), inhibition of hexokinase occurred without any hemolysis and without effects on the activity of other glycolytic enzymes. Yeast hexokinase was also inhibited by triethyltin. The red cell and yeast hexokinases were protected against inhibition by triethyltin when the sugar substrates of the enzymes were included in the incubation mixture. This work identifies hexokinase as another among a limited number of proteins that are known to interact with triethyltin.

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