PMID: 46287Mar 1, 1975

Binding properties of avian myeloblastosis virus DNA polymerases to nucleic acid affinity columns

Journal of Virology
D P Grandgenett, H M Rho

Abstract

A new method for the analysis and purification of the RNA-directed DNA polymerase of RNA tumor viruses has been developed. This nucleic acid affinity chromatography system utilizes an immobilized oligo (dT) moiety annealed with poly (A). The alpha and alphabeta DNA polymerases of avain myeloblastosis virus bound effectively to poly (A) oligo (dT)-cellulose. Alpha DNA polymerase did not bind effectively to poly (A) oligo (dT)-cellulose, poly (A)-cellulose, or to cellulose. Alphabeta bound to oligo (dT)-cellulose and cellulose at the same extent (approximately 30%), indicating that this enzyme did not bind specifically to the oligo (DT) moiety only. However, alphabeta bound to poly (A)-cellulose two to three times better than to cellulose itself, showing that alphabeta could bind to poly (A) without a primer. Alphabeta DNA polymerase also bound to poly (C)-cellulose, whereas alpha did not. These data show that the alpha DNA polymerase is defective in binding to nucleic acids if the beta subunit is not present. Data is presented which demonstrates that the alphabeta DNA polymerase bound tighter to poly (A). oligo (DT)-cellulose and to calf thymus DNA-cellulose than the alpha DNA polymerase, suggesting that the beta subunit or, at ...Continue Reading

References

Jan 1, 1992·Journal of Enzyme Inhibition·A L DeVico, M G Sarngadharan

Related Concepts

Transcription, Genetic
Rous-Associated Virus
Plasma Protein Binding Capacity
RNA Virus Infections
DNA Polymerase I
Avian myeloblastosis virus
Oligonucleotide Primers
Globin
Purification Aspects
Genetic Template

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