protomers of Na+,K+-ATPase from microsomes of duck salt gland are mostly monomeric: Formation of higher oligomers does not modify molecular activity
Author:
Publisher
Proceedings of the National Academy of Sciences
Subject
Multidisciplinary
Reference23 articles.
1. Monomer of sodium and potassium ion activated adenosine triphosphatase displays complete enzymic function
2. Soluble and enzymatically stable (Na++K+)-ATPase from mammalian kidney consisting predominantly of protomer αβ-units
3. Occlusion of 22Na+ and 86Rb+ in membrane-bound and soluble protomeric alpha beta-units of Na,K-ATPase.
4. Solubilized alpha beta Na,K-ATPase remains protomeric during turnover yet shows apparent negative cooperativity toward ATP.
5. 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
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1. Mutation of Aspartate 804 of Na+,K+-ATPase Modifies the Cation Binding Pocket and Thereby Generates a High Na+-ATPase Activity;Biochemistry;2000-07-20
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