Determination of the ATP Affinity of the Sarcoplasmic Reticulum Ca2+-ATPase by Competitive Inhibition of [γ-32P]TNP-8N3-ATP Photolabeling-Reference-Cited by-同舟云学术

Determination of the ATP Affinity of the Sarcoplasmic Reticulum Ca2+-ATPase by Competitive Inhibition of [γ-32P]TNP-8N3-ATP Photolabeling

Published:2016 Issue: Volume: Page:233-259
ISSN:1064-3745
Container-title:P-Type ATPases
language:
Short-container-title:

Author:

Clausen Johannes D.,McIntosh David B.,Woolley David G.,Andersen Jens Peter

Publisher

Springer New York

Link

http://link.springer.com/content/pdf/10.1007/978-1-4939-3179-8_22

Reference49 articles.

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2. Lacapere JJ, Guillain F (1993) The reaction mechanism of Ca(2+)-ATPase of sarcoplasmic reticulum. Direct measurement of the Mg.ATP dissociation constant gives similar values in the presence or absence of calcium. Eur J Biochem 211(1-2):117–126

3. Norby JG, Jensen J (1971) 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. Biochim Biophys Acta 233(1):104–116

4. Hegyvary C, Post RL (1971) Binding of adenosine triphosphate to sodium and potassium ion-stimulated adenosine triphosphatase. J Biol Chem 246(17):5234–5240

5. Fedosova NU, Champeil P, Esmann M (2003) Rapid filtration analysis of nucleotide binding to Na,K-ATPase. Biochemistry 42(12):3536–3543

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