Add time:07/19/2019         Source:sciencedirect.com

SummaryThe activity of calmodulin-activated cyclic nucleotide phosphodies-terase in a standard reaction containing 40 ng calmodulin could be inhibited about 50% by 14 μM Triton x-100. In contrast, the calmodulin-independent phosphodiesterase required a much higher concentration of the detergent, 380 μM for 50% inhibition of its activity. The potent inhibitory effect of Triton X-100 on the calmodulin-activated phosphodiesterase reaction could be reversed by high concentrations of calmodulin. Using the gel filtration technique, it was demonstrated that 3H-Triton X-100 bound to calmodulin with high affinity in buffer containing Ca2+. The binding of the detergent to calmodulin was mostly eliminated in the presence of trifluoperazine, a neuroleptic drug. Among other detergents examined, including Lubrol WX, Triton QS and Triton CF, only Triton CF exhibited preferential inhibition of the calmodulin-activated phosphodiesterase. The results suggest that certain detergents in the Triton family inhibit calmodulin action by undergoing Ca2+-dependent binding to the protein at the neuroleptic drug site.

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