Adenosine triphosphate phosphoydrolase activity associated with purified parainfluenza type 3 virions.
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.
D000244:Adenosine Diphosphate / Q000096:biosynthesis; D000249:Adenosine Monophosphate / Q000096:biosynthesis; D000251:Adenosine Triphosphatases / Q000378:metabolism*; D002118:Calcium / Q000494:pharmacology; D002413:Cations, Divalent; D006358:Hot Temperature; D006801:Humans; D007700:Kinetics; D008094:Lithium / Q000494:pharmacology; D008274:Magnesium / Q000494:pharmacology; D008623:Mercaptoethanol / Q000494:pharmacology; D010042:Ouabain / Q000494:pharmacology; D010224:Parainfluenza Virus 3, Human / Q000201:enzymology* / Q000302:isolation & purification; D011136:Polysorbates / Q000494:pharmacology; D011188:Potassium / Q000494:pharmacology; D018108:Respirovirus / Q000201:enzymology*; D012964:Sodium / Q000494:pharmacology
D002413:Cations, Divalent; D011136:Polysorbates; D000249:Adenosine Monophosphate; D010042:Ouabain; D008623:Mercaptoethanol; D000244:Adenosine Diphosphate; D008094:Lithium; D012964:Sodium; D000251:Adenosine Triphosphatases; D008274:Magnesium; D011188:Potassium; D002118:Calcium