Asymmetric orientation of amino groups in the α-subunit and the β-subunit of (Na+ + K+)-ATPase in tight right-side-out vesicles of basolateral membranes from outer medulla
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference25 articles.
1. Sodium and potassium ion pump in kidney tubules.
2. Purification and characterization of (Na+ + K+)-ATPase. I. The influence of detergents on the activity of (Na+ + K+)-ATPase in preparations from the outer medulla of rabbit kidney
3. Infrastructure of Na,K-ATPase in Plasma Membranes Vesicles
4. Characterization of right-side-out membrane vesicles rich in (Na,K)-ATPase and isolated from dog kidney outer medulla.
5. The labelling of proteins to high specific radioactivities by conjugation to a 125I-containing acylating agent. Application to the radioimmunoassay
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1. Cell Surface Expression of a Specific Antigenic Site on the Catalytic Subunit of (Na+ + K+)-ATPase;Biochemical and Biophysical Research Communications;2002-02
2. The thermal unfolding and domain structure of Na+/K+-exchanging ATPase.;European Journal of Biochemistry;2001-10-01
3. A unique phospholipid organization in bovine erythrocyte membranes;Proceedings of the National Academy of Sciences;2001-06-26
4. Uptake of reconstituted Na,K-ATPase vesicles by isolated lymphocytes measured by FACS, confocal microscopy and spectrofluorometry;Cell Biochemistry and Biophysics;1999-10
5. Characterisation of tissue-specific oligosaccharides from rat brain and kidney membrane preparations enriched in Na+,K+-ATPase;Glycoconjugate Journal;1999
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