[The role of the substrate structure in the function of Na,K-ATPase].

The mechanism of Na,K-ATPase function is reviewed. The peculiarities of hydrolysis of various substrates are described. The experimental results testify to the effect of substrate structure on the E2----E1 transition, rate of Na+ transport, K-dependent phosphatase activation and the quaternary structure of Na,K-ATPase.

[Study of the interaction of Na+,K+-ATPase protomers using the molecular target method].

The radiation inactivation analysis of Na+, K+-ATPase, (EC 3.6.1.

[Na,K-ATPase from the outer kidney medulla of spontaneously hypertensive rats in ontogenesis].

Specific activity of Na,K-ATPase from kidney outer medulla microsomes of spontaneously hypertensive rats (SHR) and of normotensive Kyoto-Wistar rats (WKY) at different stages of ontogenesis was studied. A positive correlation was observed between the blood pressure level and specific Na,K-ATPase activity in SHR kidney medulla. At the malignant stage of the disease, the specific activity of Na,K-ATPase exceeded that of control by 67%.

Na+ transport by reconstituted Na+,K+-ATPase in the presence of various nucleotides.

The ability of ATP, CTP, ITP, GTP, UTP and two synthetic ATP analogs to provide for ouabain-sensitive Na+ accumulation into proteoliposomes with a reconstituted Na+,K+-ATPase (ATP phosphohydrolase, EC 3.6.1.