title: Characterization of a p30 fraction from Rauscher leukemia virus which has an associated ATPase activity.
abstract: The p30 antigen from Rauscher leukemia virus (R-MuLV) was separated into two fractions by chromatography on either phosphocellulose or DEAE-cellulose. The p30-I and p30-II were indistinguishable immunologically or by isoelectrofocusing and gel electrophoresis. An ATPase activity was tightly associated with p30-II that could not be separated by ion-exchange chromatography, isoelectrofocusing, or glycerol velocity gradient sedimentation. The ATPase hydrolyzed the gamma phosphate from only ATP or dATP. Immunoglobulin directed against R-MuLV p30 completely inhibited the p30-II associated ATPase. Glycerol velocity gradient analysis showed that p30-I sedimented as a 30-kDa species while the p30-II and its associated ATPase sedimented as a 60-kDa species. The p30-II was converted entirely to a 30-kDa form by treatment with 0.2% (w/v) lithium dodecyl sulfate, suggesting that it represented a complexed species of p30. Finally, p30-II was found to stimulate the activity of R-MuLV reverse transcriptase, but p30-I had no effect on the activity of the enzyme. These results suggested the existence of at least two different forms of p30 in R-MuLV.
mesh_terms: D000251:Adenosine Triphosphatases / Q000302:isolation & purification*; D000818:Animals; D000956:Antigens, Viral / Q000302:isolation & purification*; D002460:Cell Line; D002848:Chromatography, DEAE-Cellulose; D004591:Electrophoresis, Polyacrylamide Gel; D020558:GTP Phosphohydrolases / Q000302:isolation & purification; D007525:Isoelectric Focusing; D051379:Mice; D008970:Molecular Weight; D012194:RNA-Directed DNA Polymerase / Q000302:isolation & purification; D011863:Radioimmunoassay; D011925:Rauscher Virus / Q000201:enzymology*
chemical_list: D000956:Antigens, Viral; D012194:RNA-Directed DNA Polymerase; D000251:Adenosine Triphosphatases; D020558:GTP Phosphohydrolases