Some properties of the adenosine triphosphatase associated with herpes simplex virus and nuclear membrane of host cells.
An enzyme capable to split adenosine triphosphate (ATP) was shown to be firmly associated with mature herpes simplex virus particles purified from infected rabbit lung (ZP) cells. The enzyme localized in the viral envelope was markedly activated by bivalent cations, to the largest degree by Mg2+ at a pH optimum of 7.8--8.0. Na+ and K+ ions neither separately nor together showed any activating effect. Enzyme activity was not sensitive to the action of ouabain. No adenosine diphosphatase (ADPase) and adenosine monophosphatase (AMPase) activities were observed. ATPase activity was competitively inhibited by ADP. AMP and inorganic phosphate were without effect. The ATPase of nuclear membranes isolated from ZP cells exhibited similar properties but behaved differently to the action of sodium dithionite, dinitrophenol, oligomycin and gramicidin, as well as on heat inactivation. The origin of the virus enzyme is discussed.
D000244:Adenosine Diphosphate / Q000494:pharmacology; D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D002460:Cell Line; D006863:Hydrogen-Ion Concentration; D008274:Magnesium / Q000494:pharmacology; D009685:Nuclear Envelope / Q000201:enzymology*; D011188:Potassium / Q000494:pharmacology; D018139:Simplexvirus / Q000201:enzymology*; D012964:Sodium / Q000494:pharmacology; D013696:Temperature
D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D012964:Sodium; D000251:Adenosine Triphosphatases; D008274:Magnesium; D011188:Potassium