Purification and characterization of recombinant equine infectious anemia virus reverse transcriptase. Academic Article

abstract

• A 1.67-kb segment of the equine infectious anemia virus pol gene, encoding a 66-kDa reverse transcriptase (RT), was cloned and expressed in Escherichia coli. Recombinant RT, purified by a combination of metal chelate affinity chromatography and ion-exchange chromatography, displays both RNA-dependent DNA polymerase and RNase H activity. The affinity of purified RT for its replication primer, tRNA(3Lys) was equivalent to that observed for human immunodeficiency virus RT. Our data suggest that an additional domain between RT-RNase H and integrase on the equine infectious anemia virus pol open reading frame is not an integral component of the RT polypeptide.

authors

• Payne, Susan

published proceedings

• J Virol

altmetric score

• 3

author list (cited authors)

• Le Grice, S. F., Panin, M., Kalayjian, R. C., Richter, N. J., Keith, G., Darlix, J. L., & Payne, S. L.

citation count

• 18

complete list of authors

• Le Grice, SF||Panin, M||Kalayjian, RC||Richter, NJ||Keith, G||Darlix, JL||Payne, SL

publication date

• December 1991

publisher

• American Society for Microbiology  Publisher

published in

• Journal of Virology  Journal

keywords

• Animals
• Base Sequence
• Chromatography, Ion Exchange
• Cloning, Molecular
• Escherichia Coli
• Genes, Pol
• Genes, Viral
• Horses
• Infectious Anemia Virus, Equine
• Kinetics
• Molecular Sequence Data
• Molecular Weight
• Oligodeoxyribonucleotides
• Open Reading Frames
• Polymerase Chain Reaction
• RNA-Directed DNA Polymerase
• Recombinant Proteins
• Ribonuclease H

Digital Object Identifier (DOI)

• 10.1128/JVI.65.12.7004-7007.1991

start page

• 7004

end page

• 7007

volume

• 65

issue

• 12

URL

• http://dx.doi.org/10.1128/jvi.65.12.7004-7007.1991

user-defined tag

• 3 Good Health and Well-Being