
Activity of transport ATPases was studied in erythrocyte membranes and synaptosomal fraction of cervical department of spinal cord obtained from rats in dynamics of botulinic C intoxication Na+, K+-ATPase was inhibited by the competitive type in the synaptosomal brain fraction at the preclinical period of intoxication and by the noncompetitive type at the step of skeletal muscle paresis. In erythrocyte membranes activity of Na+, K+-ATPase was inhibited by the mixed type at the preclinical period of intoxication and the enzymatic activity was inhibited by the noncompetitive type at the step of skeletal muscle paresis. The Na+, K+-ATPase from biological membranes was reactivated by unithiol and nicotinamide in dynamics of intoxication. The toxin was shown to activate Mg2+-ATPase in brain synaptosomal fraction.
Adenosine Triphosphatases, Botulinum Toxins, Hydrolysis, Erythrocyte Membrane, Synaptic Membranes, Botulism, Rats, Kinetics, Spinal Cord, Animals, Ca(2+) Mg(2+)-ATPase, Sodium-Potassium-Exchanging ATPase
Adenosine Triphosphatases, Botulinum Toxins, Hydrolysis, Erythrocyte Membrane, Synaptic Membranes, Botulism, Rats, Kinetics, Spinal Cord, Animals, Ca(2+) Mg(2+)-ATPase, Sodium-Potassium-Exchanging ATPase
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