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).