Independent Access of Fluorescein Isothiocyanate and Co(NH3)4ATP to Their Binding Sites on the Protomer of Na,K-ATPase

Author:

CAVIERES J. D.,HADDOW J.

Publisher

Wiley

Subject

History and Philosophy of Science,General Biochemistry, Genetics and Molecular Biology,General Neuroscience

Reference6 articles.

1. Shift to the Na+ form of Na+/K+-transporting ATPase due to modification of the low-affinity site by Co(NH3)4ATP;Scheiner-Bobis;Eur. J. Biochem.,1989

2. Na+/K+-ATPase with a blocked E1ATP site still allows backdoor phosphorylation of the E2ATP site;Linnertz;Eur. J. Biochem.,1995

3. Evidence for two distinct ATP sites in Na,K-ATPase purified from pig kidney;Ward;J. Physiol.,1994

4. Binding of 2′(3′)-O-(2,4,6-trinitrophenyl)ADP to soluble αβ protomers of Na,K-ATPase modified with fluorescein isothiocyanate: evidence for two distinct nucleotide sites;Ward;J. Biol. Chem.,1996

5. Purification and characterization of (Na++ K+)-ATPase;Jorgensen;III. Purification from the outer medulla of mammalian kidney after selective removal of membrane components by sodium dodecylsulphate. Biochim. Biophys. Acta,1974

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