Inhibition of alkaline phosphatase by bismuth.

The interaction of alkaline phosphatase (EC 3.1.3.1) with bismuth was studied. Among the tested alkaline phosphatases, bismuth was found to be the most effective inhibitor of the placental enzyme. Partial denaturation of the placental enzyme by papain digestion had little effect, if any, on the inhibition. Bismuth inhibition of the placental enzyme activity was more progressive with mixed glycosidase treatment than with sialidase treatment. The pH activity profile of the mixed glycosidase-treated placental enzyme was clearly shifted in the presence of bismuth. The mixed glycosidase-treated placental enzyme/bismuth mixture was more heat labile than the non-treated placental enzyme. Based on the results of kinetic studies, the inhibition mechanism of the placental enzyme by bismuth was shown to be of the competitive type, and the Ki value and Hill coefficient of the mixed glycosidase-treated placental enzyme was found to be 92 mu mol/l and 2.25, respectively. L-Phenylalanine does not interfere with the inhibitory effect of bismuth on alkaline phosphatase. Inorganic phosphate, on the other hand, appears to disturb bismuth bindings.