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

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.

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

  • 17

publication date

  • January 1991