Photoaffinity labelling of a small protein component of a purified (Na+-K+)ATPase-Reference-Cited by-同舟云学术

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Photoaffinity labelling of a small protein component of a purified (Na+-K+)ATPase

Published:1979-02-15 Issue:2 Volume:98 Page:373-376
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Rogers Terry B.,Lazdunski Michel

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(79)80220-3/fullpdf

Reference9 articles.

1. Characterization of a new photoaffinity derivative of ouabain: labeling of the large polypeptide and of a proteolipid component of the (sodium-potassium ion)-dependent ATPase

2. A simple procedure for the preparation of highly purified (sodium + potassium) adenosinetriphosphatase from the rectal salt gland of Squalus acanthias and the electric organ of Electrophorus electrieus

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2. Mechanisms of sodium pump regulation;American Journal of Physiology-Cell Physiology;2000-09-01

3. Solubilization of a Complex of Tryptic Fragments of Na,K-ATPase Containing Occluded Rb Ions and Bound Ouabain;Biochemistry;1996-01-01

4. Ouabain Binding, ATP Hydrolysis, and Na+,K+-Pump Activity During Chemical Modification of Brain and Muscle Na+,K+-ATPase;Journal of Neurochemistry;1992-03

5. Na+,K+-ATPase lsoforms in the Retina;International Review of Cytology;1992

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