The effect of monovalent and divalent cations on the ATP-dependent Ca2+-binding and phosphorylation during the reaction cycle of the sarcoplasmic reticulum Ca2+-transport ATPase
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1987.tb11435.x/fullpdf
Reference34 articles.
1. On the mechanism of Ca2+-dependent adenosine triphosphatase of sarcoplasmic reticulum. Occurrence of two types of phosphoenzyme intermediates in the presence of KCl.
2. Reaction mechanism of Ca2+-dependent ATP hydrolysis by skeletal muscle sarcoplasmic reticulum in the absence of added alkali metal salts. I. Characterization of steady state ATP hydrolysis and comparison with that in the presence of KCl.
3. Reaction mechanism of Ca2+-dependent ATP hydrolysis by skeletal muscle sarcoplasmic reticulum in the absence of added alkali metal salts. II. Kinetic properties of the phosphoenzyme formed at the steady state in high Mg2+ and low Ca2+ concentrations.
4. Phosphoenzyme formation from ATP in the ATPase of sarcoplasmic reticulum. Effect of KCl or ATP and slow dissociation of ATP from precursor enzyme-ATP complex.
5. Effect of K+ on phosphorylation of the sarcoplasmic reticulum ATPase by either Pi or ATP.
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2. Ca2+ Release to Lumen from ADP-sensitive Phosphoenzyme E1PCa2 without Bound K+ of Sarcoplasmic Reticulum Ca2+-ATPase;Journal of Biological Chemistry;2010-12
3. Structural changes in the calcium pump accompanying the dissociation of calcium;Nature;2002-08
4. Pre-steady-state kinetic study of the effects of K+ on the partial reactions of the catalytic cycle of the plasma membrane Ca2+-ATPase;Biochemical Journal;1996-04-15
5. Evidence for direct involvement of the sarcoplasmic reticulum Ca2+-ATPase in a passive monovalent cation (K+/Na+) exchange;FEBS Letters;1995-12-04
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