Abstract
Summary
The in vitro and in vivo influence of K+ on the activity of rat heart and liver PAPS-sulfotransferase (P1) was tested. The P1 activity was optimal with 0.5 μmoles K+ per μg protein. The P1 activity was decreased by mild dialysis and lost by extended dialysis. The enzyme was stable when dialyzed with K+ and tests with other ions indicated K+ specificity. Rats fed purified diets with low, normal or high levels of K+ had significantly different heart taurine concentrations and P1 specific activities. These Pi specific activities became comparable to those from the rats receiving the normal K+ diet by the addition of KC1 to the assay mixture.
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