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PMID: 6267 Published · ppublish English Journal Article

Characterization of cardiac sarcoplasmic reticulum ATP-ADP phosphate exchange and phosphorylation of the calcium transport adenosine triphosphatase.

European journal of biochemistry ·Vol. 64 ·No. 1 ·1976-04-15 ·Pages 123-30

Suko J, Hasselbach W

Abstract

1. The terminal phosphate of (gamma-32P)ATP is rapidly incorporated into cardiac sarcoplasmic reticulum membranes (0.7--1.3 mumol/g protein) in the presence of calcium and magnesium. Cardiac sarcoplasmic reticulum membranes catalize an ATP-ADP phosphate exchange in the presence of calcium and magnesium. 2. Half-maximum activation of the phosphoprotein formation and ATP-ADP phosphate exchange is reached at an ionized calcium concentration of about 0.3 muM. The Hill coefficients are 1.3. 3. Transphosphorylation and ATP-ADP phosphate exchange require magnesium and are maximally activated at magnesium concentrations close to or equal to the ATP concentration. 4. The phosphoprotein level is reduced to about 45% at an ADP/ATP ratio of 0.1. The rate of calcium-dependent ATP splitting declines, whilst the rate of the calcium-dependent ATP-ADP phosphate exchange increases when the ADP/ATP ratio is varied from 0.1 to 1. The sum of both, the rate of ATP splitting and the rate of ADP-ATP phosphate exchange remains constant. 5. Phosphoprotein formation and ATP-ADP phosphate exchange are not affected by azide, dinitrophenol, dicyclohexyl carbodiimide and oubain, whilst both activities are reduced by blockade of -SH groups localized on the outside of the sarcoplasmic reticulum membrane. 6. The isolated phosphoprotein is acid stable. The trichloroacetic acid denatured 32P-labelled membrane complex is dephosphorylated by hydroxylamine, which might indicate that the phosphorylated protein is an acyl-phosphate. 7. Polyacrylamide gel elctrophoresis (performed with phenol/acetic acid/water) of phosphorylated sarcoplasmic reticulum fractions demonstrates that the 32P-incorporation occurs into a protein of about 100000 molecular weight. 8. It is suggested that the phosphoprotein represents a phosphorylated intermediate of the calcium-dependent ATPase which formation occurs as an early step in the reaction sequence of calcium translocation by cardiac sarcoplasmic reticulum similar as in skeletal muscle.

MeSH Terms
Adenosine Diphosphate/metabolism,pharmacology Adenosine Triphosphatases/metabolism Adenosine Triphosphate/metabolism Animals Anti-Bacterial Agents/pharmacology Azides/pharmacology Biological Transport, Active Calcium/metabolism,pharmacology Dicyclohexylcarbodiimide/pharmacology Dinitrophenols/pharmacology Dogs Ethylmaleimide/pharmacology Hydrogen-Ion Concentration Kinetics Magnesium/pharmacology Molecular Weight Myocardium/metabolism Ouabain/pharmacology Sarcoplasmic Reticulum/drug effects,metabolism
Chemicals
Anti-Bacterial Agents Azides Dinitrophenols Dicyclohexylcarbodiimide Ouabain Adenosine Diphosphate Adenosine Triphosphate Adenosine Triphosphatases Magnesium Ethylmaleimide Calcium
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Suko J
Hasselbach W
Article Info
Journal
European journal of biochemistry
Abbr.
Eur J Biochem
ISSN
0014-2956
Published
1976-04-15
Pages
123-30
Language
English
Region
England
NLM ID
0107600
Subset
IM
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