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PMID: 146711 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

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.

The Journal of biological chemistry ·Vol. 253 ·No. 5 ·1978-03-10 ·Pages 1451-7

Shigekawa M, Dougherty JP

Abstract

暂无摘要

MeSH Terms

Adenosine Triphosphatases/metabolism Adenosine Triphosphate/metabolism Animals Calcium/metabolism,pharmacology Creatine Kinase Kinetics Magnesium/pharmacology Muscles/metabolism Rabbits Sarcoplasmic Reticulum/drug effects,metabolism

Chemicals

Adenosine Triphosphate Creatine Kinase Adenosine Triphosphatases Magnesium Calcium

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Shigekawa M

Dougherty J P

Article Info

Journal

The Journal of biological chemistry

Abbr.

J Biol Chem

ISSN

0021-9258

Published

1978-03-10

Pages

1451-7

Language

English

Region

United States

NLM ID

2985121R

Subset

External Links

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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.

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