Cooperativity of the alpha beta-protomer structure in Na+,K+-ATPase functioning. A scanning microcalorimetry study

Heat denaturation of the free and ligand-bound forms of purified Na+,K+-ATPase from pig kidney is studied with the scanning microcalorimetry technique. A single two-state transition is observed during denaturation of the free enzyme, the molar concentration of the cooperatively melting units being e...

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Veröffentlicht in:	FEBS letters 1986-09, Vol.205 (2), p.185-188
Hauptverfasser:	Chetverin, A B, Khechinashvili, N N, Filimonov, V V
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Calorimetry - methods Enzyme Activation Hot Temperature Membrane Proteins - metabolism Microchemistry - methods Protein Conformation Protein Denaturation Sodium-Potassium-Exchanging ATPase - metabolism Structure-Activity Relationship Swine
Online-Zugang:	Volltext
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