Solubilization of adenosine triphosphatase associated with herpes simplex virus.
The nonionic detergent Triton X-100 was used for the solubilization of Mg2"ependent adenosine triphosphatase (Mg2+ATPase) associated with mature herpes simplex virus (HSV) particles purified from infected rabbit lung (ZP) cells. The solubilization was the best at pH 8.1 with a Triton X-100 to protein ratio of 10. The solubilized enzyme splited ATP at the greatest rate at pH from 7.9 to 8.6. pH greater than 8.6 during extraction had a deleterious effect on the enzyme. In the presence of NaCl significantly more proteins were extracted but the enzyme was slightly inhibited. No enhancement of the enzyme activity after detergent treatment and the relatively mild conditions for extraction indicated that the enzyme is not too firmly associated with the surface of the herpesvirions.
D000251:Adenosine Triphosphatases / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008274:Magnesium / Q000378:metabolism; D011092:Polyethylene Glycols; D018139:Simplexvirus / Q000201:enzymology*; D012965:Sodium Chloride / Q000494:pharmacology; D012995:Solubility
D011092:Polyethylene Glycols; D012965:Sodium Chloride; D000251:Adenosine Triphosphatases; D008274:Magnesium