Isolation and characterisation of the L cell virion DNA polymerase

Abstract

The DNA polymerase of the L-cell virion (LCV) was partially purified by chromatography on DEAE cellulose. This enzyme transcribed poly(A) . oligo (dT), poly(C) . oligo(dG), and poly(Cm) . oligo(dG), had a molecular weight of 77,000 daltons and reacted like other murine viral RNA directed DNA polymerases to anti reverse transcriptase specific IgG preparations indicating that it was probably a typical murine viral reverse transcriptase. In addition, like other partially purified mammalian viral reverse transcriptases the LCV DNA polymerase exhibited template independent primer stimulated DNA synthesis. The significance of these results to the unusual endogenous activity of the LCV is discussed.

Demonstration of primer stimulated DNA synthesis by soluble reverse transcriptase

“…The virus associated DNA polymerase was parially purified by DEAE-cellulose chromotography and assayed, essentially as previously described (6).…”