Reaction mechanism of Ca2+-dependent ATP hydrolysis by skeletal muscle sarcoplasmic reticulum in the absence of added alkali metal salts. III. Sequential occurrence of ADP-sensitive and ADP-insensitive phosphoenzymes.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference13 articles.
1. 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.
2. 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.
3. Stability Constants of Metal-ion Complexes;Sillen,1964
4. Some kinetic properties of phosphorylated ATPase of sarcoplasmic reticulum formed in the absence of added alkali metal salts
5. Biochemical Aspects of Active Transport
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