Characterization of the RNA dependent DNA polymerase of a new human T-lymphotropic retrovirus (lymphadenopathy associated virus).
We described here the characteristics of the Reverse Transcriptase activity associated with the Lymphadenopathy Associated Virus ( LAV ). A critical concentration of non ionic detergent, all four deoxyribonucleosides triphosphates and the divalent cation Mg2+ are required for optimal endogenous enzyme activity. The endogenous reaction product is digested by DNase and not by RNase and its synthesis is only slightly inhibited by actinomycin D. Exogenous reactions are optimal using poly A oligo dT12 -18 or poly Cm oligo dG12 -18 as template primer and Mg2+ as divalent cation. This enzyme can be distinguished from other cellular DNA polymerases activities and from Terminal deoxynucleotidyl Transferase (TdT) by purification from LAV infected T lymphocytes using phosphocellulose column.
D055598:Chemical Phenomena; D002621:Chemistry; D002850:Chromatography, Gel; D017977:Deltaretrovirus / Q000201:enzymology*; D006801:Humans; D012194:RNA-Directed DNA Polymerase / Q000302:isolation & purification*; D013601:T-Lymphocytes / Q000201:enzymology; D013698:Templates, Genetic; D014764:Viral Proteins / Q000302:isolation & purification*
D014764:Viral Proteins; D012194:RNA-Directed DNA Polymerase