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Biochemical and Immunological Properties of the Reverse Transcriptase Associated with a Hamster Retrovirus

Yale University School of Medicine, Department of Ophthalmology and Visual Science, New Haven, Connecticut, U.S.A.

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 (i) is more active with Mn²⁺ than Mg²⁺, (ii) uses the reverse transcriptase-specific poly(rCm).oligo(dG) template, (iii) possesses substantial endogenous polymerase activity and (iv) 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 70000 mol. wt. polypeptide in highly purified virions and with 70000 and 85000 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 70000 and 85000 by glycerol density-gradient sedimentation. The HaRV reverse transcriptase and p30 were found to be most closely related antigenically to other rodent retrovirus proteins.

^* Present address: National Eye Institute, National Institutes of Health, Bethesda, Maryland, U.S.A.

Received 11 July 1979; accepted 9 November 1978.

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