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.-Reference-Cited by-同舟云学术

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.

Published:1978-03 Issue:5 Volume:253 Page:1451-1457
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Shigekawa M.,Dougherty J.P.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference19 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. Stability Constants of Metal-ion Complexes;Sillen,1964

3. A simple method for the preparation of 32P-labelled adenosine triphosphate of high specific activity

4. Reaction Mechanism of the Ca2+-dependent ATPase of Sarcoplasmic Reticulum from Skeletal Muscle: V. Vectorial Requirements for Calcium and Magnesium Ions of Three Partial Reactions of ATPase: Formation and Decomposition of a Phosphorylated Intermediate and ATP-Formation from ADP and the Intermediate*

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