. . . "P(GD303/09/H048), P(NT11071)" . "4"^^ . . . . "http://www.sciencedirect.com/science/article/pii/S1388248112005024" . . "2"^^ . "Changes in the intrinsic electrocatalytic nature of Na /K ATPase reflect structural changes on ATP-binding: Electrochemical label-free approach" . "Structural changes; Sodium-potassium pum; Membrane protein; Mercury electrode; Chronopotentiometry; Electroanalysis"@en . "Changes in the intrinsic electrocatalytic nature of Na /K ATPase reflect structural changes on ATP-binding: Electrochemical label-free approach" . "Kubala, Martin" . "15310" . "US - Spojen\u00E9 st\u00E1ty americk\u00E9" . . . . . "1388-2481" . . "Vacek, Jan" . . "Havl\u00EDkov\u00E1, Marika" . "[C4740016F2EC]" . "Changes in the intrinsic electrocatalytic nature of Na /K ATPase reflect structural changes on ATP-binding: Electrochemical label-free approach"@en . . "Changes in the intrinsic electrocatalytic nature of Na /K ATPase reflect structural changes on ATP-binding: Electrochemical label-free approach"@en . "Chronopotentiometric stripping (CPS) analysis was used to show that transmembrane protein Na+/K+-ATPase (NKA) structural changes can be observed in the presence of ATP. The ATP-induced structural changes lead to modulation of NKA ability to catalyze the hydrogen evolution on Hg-electrode. The electrochemical data on NKA are compared to monitoring of changes in intrinsic fluorescence and discussed with respect to crystallographic structures of homologous sarco/endoplasmic reticulum Ca2+-ATPase (SERCA). The results show that CPS analysis of intrinsic electroactivity (label-free approach) could be applied for monitoring of structural changes and molecular interactions of membrane proteins, such as NKA." . "Zatloukalov\u00E1, Martina" . "5"^^ . . "Ulrichov\u00E1, Jitka" . . "Chronopotentiometric stripping (CPS) analysis was used to show that transmembrane protein Na+/K+-ATPase (NKA) structural changes can be observed in the presence of ATP. The ATP-induced structural changes lead to modulation of NKA ability to catalyze the hydrogen evolution on Hg-electrode. The electrochemical data on NKA are compared to monitoring of changes in intrinsic fluorescence and discussed with respect to crystallographic structures of homologous sarco/endoplasmic reticulum Ca2+-ATPase (SERCA). The results show that CPS analysis of intrinsic electroactivity (label-free approach) could be applied for monitoring of structural changes and molecular interactions of membrane proteins, such as NKA."@en . . . "64942" . "RIV/61989592:15310/13:33143456" . . "FEB" . . "27" . "Electrochemistry Communications" . . "RIV/61989592:15310/13:33143456!RIV14-MZ0-15310___" .