pH-Dependent Change in the Oligomeric Structure of the Solubilized Na+/K+-ATPase
Author:
Publisher
Wiley
Subject
History and Philosophy of Science,General Biochemistry, Genetics and Molecular Biology,General Neuroscience
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1749-6632.1997.tb52239.x/fullpdf
Reference5 articles.
1. Minimum enzyme unit for Na+/K+-ATPase is the αβ-protomer. Determination by low-angle laser light scattering photometry coupled with high-performance gel chromatography for substantially simultaneous measurement of ATPase activity and molecular weight
2. [28] Membrane protein molecular weight determined by low-angle laser light-scattering photometry coupled with high-performance gel chromatography
3. Change in oligomeric structure of solubilized Na+ /K+-ATPase induced by octaethylene glycol dodecyl ether, phosphatidylserine and ATP
4. EFFECT OF ATP ON Na: K AFFINITY AND CATALYTIC ACTIVITY OF (Na++ K+)-ACTIVATED ENZYME SYSTEM
5. A pH induced two-dimensional crystal of membrane-bound Na+ ,K+ -ATPase of dog kidney
Cited by 2 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Na+- and K+-Dependent Oligomeric Interconversion among -Protomers, Diprotomers and Higher Oligomers in Solubilized Na+/K+-ATPase;Journal of Biochemistry;2007-05-23
2. Kinetic characterization of Na,K-ATPase from rabbit outer renal medulla: properties of the (αβ)2 dimer;Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology;2003-07
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