T. O. Veklich¹, A. A. Shkrabak¹, Yu. Yu. Mazur¹,
R. V. Rodik², V. I. Kalchenko², S. O. Kosterin¹

¹Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv;
²Institute of Organic Chemistry, National Academy of Sciences of Ukraine, Kyiv;
e-mail: kinet@biochem.kiev.ua; vik@ioch.kiev.ua

In experiments on the suspension of myometrium cell plasma membrane, processed by 0.1% digitonin, the inhibitory action of calix[4]arene C-90 (5,11,17,23-tetra(threeftor)methyl(phenilsulphonilimino)-methylamino-25,26, 27,28-tetrapropoxy-calix[4]arene) on the activi­ty of Ca²⁺,Mg²⁺-ATPase was investigated. The authors also examined the influence of calix[4]arene in different concentration on affinity of enzyme (Ca²⁺,Mg²⁺-ATPase) for the ATP and ions of Mg and Ca, and its influence on cooperative effect and maximum velocity of ATP hydrolysis. It is shown that calix[4]arene does not influence the affinity of Ca²⁺,Mg²⁺-ATPase for the ATP, which means that these two compounds have different binding centers­. Also calix[4]arene has no influence on affinity and cooperative effect of Ca ions, if it is used in concentration lower than 50 µM. Calix[4]arene slightly increases coefficient of Ca²⁺,Mg²⁺-ATPase activation by magnesium chloride. In all three cases, where ATP, Mg and Ca ions are used to test the impact of calix[4]arene, maximum velocity of ATP hydrolysis significantly decreases. All these results clarify that calix[4]arene implements its inhibitory action through mechanism of uncompetitive inhibition of Ca²⁺,Mg²⁺-ATPase activity.