Abstract
Abstract 19 F NMR spectra were measured to investigate the interaction of trifluoperazine (TFP) with porcine brain S100 protein (S100) under various conditions. It was found that TFP binds to S100 irrespective of Ca 2+ . However, in the presence of Ca 2+ the apparent affinity of TFP to protein ( K d = 20 μM) was greater than that in its absence ( K d = 85 μM). Zn 2+ also enhanced the binding of TFP to S100. The ratio of TFP bound to S100 was estimated to be nearly unity in the presence of Ca 2+ . It was also found that KCl only markedly affected the interaction of TFP with S100 in the presence of Ca 2+ . The 19 F NMR chemical shift of the TFP-S100 solution changed much depending upon the pH of the solution in the presence of Ca 2+ , while no remarkable pH dependence of the 19 F NMR chemical shift was observed for the TFP-S100 solution in the absence of Ca 2+ . These pH effects are in contrast wih those observed for the TFP-calmodulin solution.
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