Purification and characterization of DNA polymerases from the plasmacytoma MOPC 104E and Abelson murine leukemia viruses.
RNA-dependent DNA polymerases of intracisternal A particles from the mouse plasma cell tumor MOPC 104E and of Abelson murine leukemia virus (A-MuLV) were isolated from particle preparations by Nonidet P40 and ultrasonic treatment and purified by column chromatography on DEAE-cellulose and phosphocellulose, followed by centrifugation in linear sucrose gradients. Both DNA polymerases were very similar in their elution patterns from phospho and DEAE-cellulose, template specificities, requirements for optimum activity and inactivation by anti-(reverse transcriptase) antiserum. They are associated with ribonuclease H activity. For molecular weight determinations, antibody-precipitated enzymes were bound to staphylococcal-protein-A-Sepharose, solubilized and run on dodecylsulfate/polyacrylamide gels. Their apparent molecular weight was estimated to be 80000.
D000818:Animals; D002460:Cell Line; D004259:DNA-Directed DNA Polymerase / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D009052:Leukemia Virus, Murine / Q000201:enzymology*; D051379:Mice; D008970:Molecular Weight; D010954:Plasmacytoma / Q000201:enzymology / Q000648:ultrastructure
D004259:DNA-Directed DNA Polymerase