Purification and characterization of DNA polymerases from the plasmacytoma MOPC 104E and Abelson murine leukemia viruses.

Abstract

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.

• Authors: B J Weimann, J Schmidt, B Takacs
• Journal: European journal of biochemistry (Eur J Biochem) Vol. 85 Issue 2 Pg. 571-9 (Apr 17 1978) ISSN: 0014-2956 [Print] England
• PMID: 206440 (Publication Type: Journal Article)

Chemical References

• DNA-Directed DNA Polymerase

Topics

• Animals
• Cell Line
• DNA-Directed DNA Polymerase (isolation & purification, metabolism)
• Kinetics
• Leukemia Virus, Murine (enzymology)
• Mice
• Molecular Weight
• Plasmacytoma (enzymology, ultrastructure)