Autor:	Z P, Kometiani, M G, Vekua
Rok vydání:	1983
Předmět:	Kinetics Adenosine Triphosphate Binding Sites Sodium Methods Potassium Animals Brain Cations Monovalent Sodium-Potassium-Exchanging ATPase Protein Binding Rats
Zdroj:	Biokhimiia (Moscow, Russia). 48(6)
ISSN:	0320-9725
Popis:	An analysis of the shapes of the kinetic curves for the cationic sites of the Na,K-ATPase system revealed four completely activated Na-sites. Free ATP can change the so-called operation regime of Na,K-ATPase. At ATP excess two completely activated K-sites are detected, whereas at low ATP concentrations only one incompletely activated site is observed.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::fd030119440105382922fdd8c7c112ea https://pubmed.ncbi.nlm.nih.gov/6309255 Zobrazit plný text záznamu