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