Publications by authors named "V K Turmukhambetova"

The effects of the cholinergic agonist carbachol (Cch) and guanine nucleotides on the Na,K-ATPase and K-dependent p-nitrophenylphosphatase (K-p-NPPase) activities in rabbit and dog myocardial sarcolemma vesicles in the presence of the pore-forming antibiotic alamethicin (20 micrograms/ml), was studied. Cch (0.01-100 microM) inhibited the both enzymatic activities by 40-45% (IC50 = 0.

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The cholinergic agonist carbachol produces a concentration-dependent (half-maximum inhibitory concentration = 0.9 microM) decrease in the Na(+)-K(+)-adenosine triphosphatase (ATPase) activity of rabbit cardiac sarcolemma that occurred only in the presence of guanosine 5'-[gamma-thio]triphosphate (0.1 microM GTP gamma S) and reached 40% inhibition.

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Acetylcholine (10(-7)-10(-2) M) enhanced the Na+, K+-ATPase activity in sarcolemmal vesicles from myocardium and intestinal smooth muscle. The stimulation of the enzyme from canine ventricles reaches 150% and was less pronounced (10-20%) in the case of frog myocardium and canine ileal muscles. The activating action of the neurotransmitter was simulated by gramicidin D (1-5 microM), but not by valinomycin 1-5 microM), blocked both by ouabain (200 microM) and atropine (0.

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Acetylcholine does not change the activity of Na, K-ATPase isolated from pig kidney. The enzyme is shown to have insignificant acetylcholinesterase activity. It is suggested that Na, K-ATPase sensitivity to acetylcholine disappears in the course of enzyme purification and that acetylcholinesterase activity is extrinsic.

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Acetylcholine (ACH) produced specific inhibition of Na, K-ATP-ase activity in sarcolemmic preparations of the frog heart (K0.5 = 1 microM), dog atria (K0,5 = 5 microM) and ventricles (K0.5 = 1 microM), and dog small intestinal smooth muscles (K0,5 = 0.

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