Abstract
The chromatographic behavior of DNA polymerase activity in solubilized preparations of Rauscher murine leukemia virus (R-MuLV), murine mammary tumor virus (MuMTV), Mason-Pfizer monkey virus (MP-MV), and avian myeloblastosis virus (AMV) was examined on agarose derivatives containing hydrocarbon arms of various lengths. Ethyl-(C 2)- and hexylimino-(C 6)-agarose failed to bind significant quantitites of DNA polymerase activity. R-MuLV DNA polymerase bound to octylimino-(C 8)- and decylimino-(C 10)-agarose, and could be quantitatively recovered from these matrices by elution with buffers containing ethylene glycol alone and in the presence of detergents, respectively. The other viral polymerases demonstrated equal or greater affinities for these matrices. The potential for hydrophobic interaction by viral DNA polymerases revealed by our studies provides a mechanism whereby the specific complexing of reverse transcriptase with retroviral structural proteins in the absence of RNA may be explained.
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