[Binding of Rb86 by a microsomal fraction of bovine cerebral cortex cells].

The maximal binding of 86Rb was noted when ions of Mg, ATP and Na were present simultaneously. The availability of olytoriside (1-10(-4)M), CaCl2 (1-10(-3)M) and phospholipase A (1-10(-5)M) in the medium and the removal of Na and substitution of ATP for ADP decreased to a different extent the binding of 86Rb.

[Tryptophan fluorescence of Na+,K+-ATPase preparations].

On the strength of the study of tryptophan fluorescence of Na+, K+-ATPase preparation a conclusion about conformational changes of the enzume molecule at the level of its tertiary structure is made. The largest changes of intensity and position of fluorescence spectrum consequently the macromolecule structure are discovered at the formation of Mg-ATP-enzyme complex.

[Role of calcium ions and fatty acids in the inhibition of Mg2+, Na+ and K+-ATPases by means of the "direct" hemolysin and phospholipase A of cobra venom].

The influence of calcium ions and fatty acids in the action of direct hemolytic factor and phospholipase A on Mg2+ and Na+, K+-ATPases was investigated. It was established that calcium activates greatly phospholipase A and to a less extent--the direct hemolytic factor. The activity of ATPases is inhibited most effectively by the system consisting of phospholipase A, direct hemolytic factor and Ca2+.