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Eur J Pharmacol. 1996 Aug 22;310(1):95-8.

Ptilomycalin A, a novel Na+, K(+)- or Ca2(+)-ATPase inhibitor, competitively interacts with ATP at its binding site.

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  • 1Department of Pharmaceutical Molecular Biology, Faculty of Pharmaceutical Sciences, Tohoku University, Sendai, Japan.


Ptilomycalin A inhibited the brain Na+, K(+)-ATPase and Ca2(+)-ATPase from skeletal sarcoplasmic reticulum with an IC50 value of 2 microM and 10 microM, respectively. Kinetic analysis of the inhibitory effects of ptilomycalin A suggests that the inhibition of Na+, K(+)-ATPase is a competitive-, an uncompetitive- and an anticompetitive-type with respect to ATP, Na+ and K+, respectively. The inhibition of Ca2(+)-ATPase by ptilomycalin A is a competitive- or an uncompetitive-type with respect to ATP or Ca2+, respectively. These results suggest that ptilomycalin A interacts with ATP at the ATP binding site of Na+, K(+)-ATPase or Ca2(+)-ATPase. Ptilomycalin A has become a useful biochemical tool for clarifying the ATP binding site in both enzymes.

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