KINETIC REGULARITIES AND MECHANISMS OF ACTION OF?CALIXARENE C-99
ON? ATPase ACTIVITY OF MYOSIN SUBFRAGMENT-1 OF MYOMETRIUM
1Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv;
2Institute of Organic Chemistry, National Academy of Sciences of Ukraine, Kyiv;
It has been shown that calixarene C-99 inhibited myosin subfragment-1 ATPase of myometrium. This inhibition is noncompetitive as to ATP and Mg2+. At the same time, this compound reduces the seeming enzymatic hydrolysis maximum rate of nucleoside triphosphate with respect to ATP and Mg2+.
With the help of computer design the interaction of mentioned calixarene with myosin subfragment-1 of myometrium has been investigated. Several mechanisms involved in the calixarene C-99 inhibition of myosin head ATPase were supposed and participation of hydrogen, hydrophobic and electrostatic interactions in these mechanisms was discussed.
Key words: calixarenеs C-99, subfragment-1 of myosin, myometrium, smooth muscles, enzymic hydrolysis of АТР, kinetic properties of АТРаse, computer design, docking.
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