Effects of Neostigmine and Physostigmine on Activity of Na,K-ATPase in Various Subdivisions of Rat Brain.

The effects of intramuscular administration of neostigmine and physostigmine on Na,K-ATPase activity in various cerebral subdivisions were examined in rats. In CNS and peripheral tissues, both agents rapidly and significantly reduced activity of cholinesterases by 30-50%. The development of intoxication did not change the marker indices of stress reaction.

Species variability of erythrocyte transport ATPases in mammals.

Na+, K(+)-ATPase, and Ca(2+)-ATPase in whole erythrocytes from five species of mammals (rat, mouse, guinea pig, golden hamster, rabbit) after cell treatment with Tween 20 (7.5 mg/ml) varied over a wide range: from 3.0 +/- 0.

[A comparative study of the properties of ouabain-sensitive phosphatase in rat erythrocyte ghosts and spectrin-free membranes].

The removal of the membrane skeleton proteins (MSP), chiefly spectrin and actin, from the rat erythrocyte ghosts was shown to result in a decrease of both the total Na, K-ATPase activity and a partial reaction of the enzyme, namely the phosphatasic one. Besides, modulating effects of the effectors promoting the enzyme conformational transitions (ATP and Mg2+) on the ouabain-sensitive K-phosphatase is changed. For instance, a pronounced activation of the K-phosphate in a high-potassium medium in the presence of 1 mM ATP disappeared and the degree of the enzymatic activity enhancement in response to increasing MgCl2 concentrations (from 1.

[A comparative study of the intracellular regulation of transport ATPase activity in non-nucleated erythrocytes].

Removing the basic cytoskeleton proteins (spectrin, 4.1 and 2.1 band proteins) from the unnuclear erythrocyte membranes of four mammalian species (mouse, hamster, guinea, pig and rabbit) made no changes in Na,K-ATPases, while the specific activity of Ca-ATPases was decreased (the decreasing was of a range of 60-90% depending on the species, in values per mg of protein).

Some properties of erythrocyte Na+-K+-ATPase in essential hypertension.

The activity and some allosteric properties of Na+-K+-ATPase in erythrocytes and their membrane preparations (ghosts) from 57 patients with essential hypertension and 36 normotensive controls were studied. To reveal enzyme activity in whole erythrocytes the cells were pretreated with detergent Tween-20. It was found that in the patient erythrocytes the Na+-K+-ATPase activity was 33% less as compared to the control group.

[Mechanism of the activating effect of detergents and chelating agents on the Na, K-ATPase activity of erythrocyte ghosts].

The reasons for differences in the Na,K-ATPase activity in rat erythrocyte ghosts obtained by hypoosmotic hemolysis in 10 mM Tris-HCl buffer pH 7.6 in the absence ("Tris-ghosts") and presence ("EDTA-ghosts") were investigated. Structurally different detergents (Triton X-100, Tween-20 and sodium deoxycholate) taken at optimal concentrations increased the enzyme activity in a similar way, i.

[Na K ATPase activity in mammalian erythrocytes].

The effects of membranotropic substances--nonionic detergent Tween-20 and EDTA--on the activity and some properties of Na,K-ATPase from mammalian erythrocytes were studied. It was shown that pretreatment of whole erythrocytes with Tween-20 (5 mg/ml) allows a detection of the enzyme activity, which cannot be detected in intact cells. It was also found that erythrocyte ghosts with a high and stable activity of Na,K-ATPase can be obtained by injections of EDTA (1-2 mM) into the hemolysis medium.