Abstract
S100 protein exhibited an inhibitory effect on the adenosine triphosphatase activity of brain microtubule proteins in a concentration-dependent manner. In the presence of Ca2+, maximal inhibition was about 90% (only about 10% of the original activity remained), while the maximum inhibition in the presence of Mg2+ was about 30%. Zn2+, which can bind both microtubule proteins and S100 protein, had little effect on the inhibitory action of S100 protein in the presence or absence of Ca2+. The inhibition by S100 protein was reduced by chlorpromazine.
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