Abstract
An adenosine triphosphate phosphohydrolase associated with purified parainfluenza type 3 virions has been characterized. It hydrolyzed ATP to ADP and AMP when activated with Mg-2+ ions. Using Ca-2+ the production of ADP was inhibited but not that of AMP. Neither K+ NOR Na+ ions were required for the expression of maximal activity. Ouabain had no inhibitory effect on enzyme activity even at 10-3M. After exposure of virus preparations to Tween 20, enzyme activity was not affected. A linear relationship between enzyme activity and concentration of virus was observed.
MeSH terms
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Adenosine Diphosphate / biosynthesis
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Adenosine Monophosphate / biosynthesis
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Adenosine Triphosphatases / metabolism*
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Calcium / pharmacology
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Cations, Divalent
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Hot Temperature
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Humans
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Kinetics
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Lithium / pharmacology
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Magnesium / pharmacology
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Mercaptoethanol / pharmacology
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Ouabain / pharmacology
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Parainfluenza Virus 3, Human / enzymology*
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Parainfluenza Virus 3, Human / isolation & purification
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Polysorbates / pharmacology
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Potassium / pharmacology
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Respirovirus / enzymology*
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Sodium / pharmacology
Substances
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Cations, Divalent
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Polysorbates
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Adenosine Monophosphate
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Ouabain
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Mercaptoethanol
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Adenosine Diphosphate
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Lithium
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Sodium
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Adenosine Triphosphatases
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Magnesium
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Potassium
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Calcium