(Mg 2+ + K +)-Dependent inhibition of NaK-ATPase due to a contaminant in equine muscle ATP

A contaminant present in commercial ATP isolated from equine muscle induces a (Mg 2+ + K +)-dependent inhibition of human red cell NaK-ATPase (EC 3.6.1.3). This inhibition is completely reversed by isoproterenol (1 mM). The contaminant (inhibitor) is essentially lacking in ATP prepared synthetically...

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Published inBiochemical and biophysical research communications Vol. 77; no. 3; pp. 1024 - 1029
Main Authors Hudgins, Patricia M., Bond, Guy H.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 08.08.1977
Subjects
Adenosine Triphosphatases - antagonists & inhibitors
Adenosine Triphosphatases - blood
Adenosine Triphosphate - isolation & purification
Animals
Enzyme Activation
Erythrocyte Membrane - enzymology
Erythrocytes - enzymology
Horses
Humans
Isoproterenol - pharmacology
Kinetics
Magnesium - pharmacology
Muscle Proteins - isolation & purification
Muscle Proteins - pharmacology
Muscles
Potassium - metabolism
Potassium - pharmacology
Sodium - metabolism
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Summary:A contaminant present in commercial ATP isolated from equine muscle induces a (Mg 2+ + K +)-dependent inhibition of human red cell NaK-ATPase (EC 3.6.1.3). This inhibition is completely reversed by isoproterenol (1 mM). The contaminant (inhibitor) is essentially lacking in ATP prepared synthetically by phosphorylation of adenosine. A procedure is described for separation of the inhibitor from equine muscle ATP with strongly acidic cation exchange resin. In the presence of isolated inhibitor, a (Mg 2+ + K +)-dependent inhibition of NaK-ATPase can be demonstrated with synthetic ATP as the substrate.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:0006-291X
1090-2104
DOI:10.1016/S0006-291X(77)80080-6