Abstract
19F-n.m.r. spectra were measured to investigate the effects of Ca 2+ and Zn 2+ on the interaction of trifluoperazine (TFP) with three S100 proteins. It was found that TFP binds to S100a and S100a 0 proteins irrespective of the presence of Ca 2+ and Zn 2+, while in the presence of Ca 2+ the apparent affinity of TFP to the proteins was greater than that in its absence or in the presence of Zn 2+. In contrast, the binding affinity of TRP to S100b protein in the presence and absence of metal ions was lower than to S100a and S100a 0 proteins. These results suggested that TFP binds to each S100 protein in two ways; one is Ca 2+ - or Zn 2+ -dependent specific manner and another is Ca 2+ - or Zn 2+ -independent non-specific manner.
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