Kaplya O. Structural and functional properties of Na+,K+-ATP-ase catalytic subunit isoforms under membrane-disturbing influences

Na+,K+-ATP-ase membrane preparations from rat and bovine brain and kidney.The elucidation of the peculiarities of the Na+,K+-ATP-ase catalytic subunit isoform functional disoders under plasma membrane structural modification in vitro. The experimental methods: ultracentrifugation, gel-electrophoresis, autoradiography, spectrophotometry; enzymatic methods. The differences of the sensitivity of the neuronal enzyme isoforms to nonoxidative modification of the membrane lipid component were revealed. The existence of the peculiarities in the boundary lipids structural organization is suggested. The conception of local viscotropic regulation of the functional activity of the neuronal Na+,K+-ATP-ase isoforms is substuntiated. It is established that Na+,K+-ATP-ase is the direct target of the isoform-specific nonenzymatic oxidation.The results are important for correct evaluation of the pathophysiological and pharmacological membrane-disturbing influences in basic and applied investigations in neurochemical membranology and pharmacology. The field of application - scientific institutions of medico-biological type.