Studies of the template preference and other characteristics of the DNA polymerases of leukemic guinea pig lymphoblasts.
A single peak of DNA polymerase activity was detectable by phosphocellulose chromatography of leukemic guinea pig lymphoblast whole cell extracts. The inability to detect multiple peaks of activity as described with other cell types is shown to be due to the insolubility of a large proportion of the DNA polymerase activity under the extraction condition used. Multiple forms of DNA polymerase with different template specificities were recognized in extracts of the subcellular fractions of these cells after chromatography on phosphocellulose and DEAE cellulose. On Sephadex G-200 gel filtration these enzymes had apparent molecular weights in excess of 140,000 daltons. No RNA polymerase (reverse transcriptase) was detected in any subcellular fraction despite the presence of oncornavirus like particles in these cells.
D000818:Animals; D002467:Cell Nucleus / Q000201:enzymology; D003600:Cytosol / Q000201:enzymology; D004259:DNA-Directed DNA Polymerase / Q000378:metabolism*; D006168:Guinea Pigs; D007700:Kinetics; D007942:Leukemia, Experimental / Q000201:enzymology*; D007945:Leukemia, Lymphoid / Q000201:enzymology; D008214:Lymphocytes / Q000201:enzymology*; D008970:Molecular Weight; D013347:Subcellular Fractions / Q000201:enzymology; D013698:Templates, Genetic
D004259:DNA-Directed DNA Polymerase