Biochemical and immunological properties of the reverse transcriptase associated with a hamster retrovirus

D. S. Gregerson, P. Russell, T. W. Reid

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Several properties of an RNA-directed DNA polymerase associated with a hamster retrovirus (HaRV) were examined and found to be similar to other polymerases from mammalian type-C viruses in that the enzyme is more active with Mn2+ than Mg2+, uses the reverse transcriptase-specific poly(rCm).oligo(dG) template, possesses substantial endogenous polymerase activity and is strongly inhibited by homologous antisera and moderately inhibited by antisera directed against other type-C viruses. In contrast to previous reports of polymerases from other hamster viruses, HaRV polymerase is active in endogenous assays and the activity is associated with a 70,000 mol. wt. polypeptide in highly purified virions and with 70,000 and 85,000 mol. wt. polypeptides in fresh, unpurified virus. Only one major peak of polymerase activity eluted from DEAE-cellulose while subsequent elution of this peak from phosphocellulose produced two major peaks of polymerase activity. The mol. wt. of these two peaks were 70,000 and 85,000 by glycerol density-gradient sedimentation. The HaRV reverse transcriptase and p30 were found to be most closely related antigenically to other rodent retrovirus proteins.

Original languageEnglish (US)
Pages (from-to)327-337
Number of pages11
JournalJournal of General Virology
Issue number2
StatePublished - 1979


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