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dc.creatorPekovic, S
dc.creatorNedeljkovic, N
dc.creatorNikezic, G
dc.creatorHorvat, Anica
dc.creatorStojiljković, Mirjana
dc.creatorRakic, L
dc.creatorMartinović, Jelena
dc.identifier.issn0231-5882 (print)
dc.description.abstractThe activities and basic enzymatic properties of Na,K-ATPase were examined in synaptosomal plasma membranes (SPM) prepared from rat hippocampus and striatum. A kinetic analysis showed profound differences in apparent affinities for ATP (K-m) between hippocampal (1.21 mmol/l) and striatal (0.76 mmol/l) enzyme preparations, as well as in the corresponding V-max values. However, physiological efficiencies were almost the same. The complex pattern of dose-response curves to ouabain indicated the presence of two high-affinity forms of Na,K-ATPase in the striatum (very high-:K-i = 3.73 x 10(-8) mol/l and high-:K-i = 4.21 x 10(-5) mol/l), and one high affinity form in the hippocampus (K-i = 6.6 x 10(-7) mol/l). In addition, both SPM preparations contained one low affinity form with similar K-i. The very high-affinity form had positive cooperativity for ouabain inhibition of Na,K-ATPase activity, in contrast to high- and low-affinity forms, which exhibited negative cooperativity. The respective contributions of ouabain-sensitive forms to the total activity were estimated as 22%, 46%, 19% for the striatum and 36%, 45% for the hippocampus. These data clearly demonstrate striking differences in kinetic properties of the hippocampal and striatal Na,K-ATPase that may be due to the isoenzyme diversity and adaptation to specific physiological demands of the examined rat brain regions.en
dc.sourceGeneral Physiology and Biophysicsen
dc.subjectsynaptic plasma membranesen
dc.titleBiochemical characterization of the hippocampal and striatal Na,K-ATPase reveals striking differences in kinetic propertiesen
dcterms.abstractПековиц, С; Недељковиц, Н; Никезиц, Г; Ракиц, Л; Стојиљковиц, М; Хорват, Aница; Мартиновић Јелена;

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