A kinetic model for N-ethylmaleimide inhibition of the (Na+ + K+)-ATPase from rectal glands of Squalus acanthias
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference22 articles.
1. Effect of ATP on the intermediary steps of the reaction of the (Na++K+)-dependent enzyme system. I. Studied by the use of N-ethylmaleimide inhibition as a tool
2. Ligand-dependent reactivity of ( with showdomycin
3. Evidence for Two Different Reactive Sulfhydryl Groups in the ATP-Binding Sites of (Na++ K+)-ATPase
4. Effects of Cations on High-Affinity and Low- Affinity ATP-Binding Sites of (Na+, K+)-ATPase as S+tudied by Disulfides of Thioinosine Triphosphate and Its Analogue
5. The reaction of sulfhydryl groups of sodium and potassium ion-activated adenosine triphosphatase with N-ethylmaleimide. The relationship between ligand-dependent alterations of nucleophilicity and enzymatic conformational states.
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1. Indanedione spin labelling of Na,K-ATPase;Biochimica et Biophysica Acta (BBA) - Biomembranes;2002-12
2. Heterogeneity of Na;Pflügers Archiv;1999
3. Approaches to Disulfide Bonds Identification in the Na+/K+-ATPase Alpha Subunit;The Sodium Pump;1994
4. Maleimide, Iodoacetamide, Indanedione, and Chloromercuric Spin Label Reagents with Derivatized Nitroxide Rings as ESR Reporter Groups for Protein Conformation and Dynamics;Analytical Biochemistry;1993-09
5. Analysis of thiol-topography in Na,K-ATPase using labelling with different maleimide nitroxide derivatives;Biochimica et Biophysica Acta (BBA) - Biomembranes;1992-12
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