Characterization of a p30 Fraction from Rauscher Leukemia Virus
نویسندگان
چکیده
The p30 antigen from Rauscher leukemia virus (RMuLV) was separated into two fractions by chromatography on either phosphocellulose or DEAE-cellulose. The p30-I and p30-I1 were indistinguishable immunologically or by isoelectrofocusing and gel electrophoresis. An ATPase activity was tightly associated with p30-I1 that could not be separated by ion-exchange chromatography, isoelectrofocusing, or glycerol velocity gradient sedimentation. The ATPase hydrolyzed the y phosphate from only ATP or dATP. Immunoglobulin directed against R-MuLV p30 completely inhibited the p30-I1 associated ATPase. Glycerol velocity gradient analysis showed that p30-I sedimented as a 30-kDa species while the p30-I1 and its associated ATPase sedimented as a 60-kDa species. The p30-I1 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-I1 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.
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