Inactivation of (Na+,K+)-ATPase by beta-mercaptoethanol. Differential sensitivity to reduction of the three beta subunit disulfide bonds.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference30 articles.
1. Mechanism of the Na+, K+ pump protein structure and conformations of the pure
2. Assembly of the (Na+ + K+)-adenosine triphosphatase. Post-translational membrane integration of the alpha subunit.
3. Evidence for essential disulfide bonds in the β-subunit of (Na+ + K+)-ATPase
4. Protective effect of Na+ and K+ against inactivation of (Na+ + K+-ATPase by high concentrations of 2-mercaptoethanol at high temperatures
5. Amino-acid sequence of the β-subunit of the (Na+ + K+)ATPase deduced from a cDNA
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