Characterization of 2',3'-O-(2,4,6-trinitrocyclohexadienylidine)adenosine 5'-triphosphate as a fluorescent probe of the ATP site of sodium and potassium transport adenosine triphosphatase. Determination of nucleotide binding stoichiometry and ion-induced changes in affinity for ATP.-Reference-Cited by-同舟云学术

Characterization of 2',3'-O-(2,4,6-trinitrocyclohexadienylidine)adenosine 5'-triphosphate as a fluorescent probe of the ATP site of sodium and potassium transport adenosine triphosphatase. Determination of nucleotide binding stoichiometry and ion-induced changes in affinity for ATP.

Published:1981-03 Issue:5 Volume:256 Page:2346-2356
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Moczydlowski E.G.,Fortes P.A.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference69 articles.

1. Binding of Adenosine Triphosphate to Sodium and Potassium Ion-stimulated Adenosine Triphosphatase

2. Binding of ATP to brain microsomal ATPase Determination of the ATP-binding capacity and the dissociation constant of the enzyme-ATP complex as a function of K+ concentration

3. Reaction of (sodium(1+)-potassium(1+) ion)-activated ATPase with 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole: evidence for an essential tyrosine at the active site

4. Biochemistry of Membrane Transport;Post,1977

5. ATP hydrolysis associated with an uncoupled sodium flux through the sodium pump: evidence for allosteric effects of intracellular ATP and extracellular sodium

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