The effect of ionic strength and specific anions on substrate binding and hydrolytic activities of Na,K-ATPase.

Nørby, J G; Esmann, M

Nørby, J G; Esmann, M.

Affiliation

Nørby JG; Department of Biophysics, University of Aarhus, Denmark. jgn@mil.aau.dk

J Gen Physiol ; 109(5): 555-70, 1997 May.

Article in En | MEDLINE | ID: mdl-9154904

Subject(s)

Potassium/metabolism; Sodium-Potassium-Exchanging ATPase/metabolism; Sodium/metabolism; Sodium/pharmacology; 4-Nitrophenylphosphatase/metabolism; Adenosine Diphosphate/metabolism; Animals; Binding Sites; Enzyme Activation/drug effects; Eosine Yellowish-(YS)/metabolism; Fluorescent Dyes; Hydrolysis; Kidney Medulla/enzymology; Swine; Thermodynamics

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Potassium / Sodium / Sodium-Potassium-Exchanging ATPase Limits: Animals Language: En Journal: J Gen Physiol Year: 1997 Document type: Article Affiliation country: Denmark

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