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. 1991 Dec;65(12):7004-7.
doi: 10.1128/JVI.65.12.7004-7007.1991.

Purification and characterization of recombinant equine infectious anemia virus reverse transcriptase

S F Le Grice  1 , M Panin, R C Kalayjian, N J Richter, G Keith, J L Darlix, S L Payne
Affiliations

Purification and characterization of recombinant equine infectious anemia virus reverse transcriptase

S F Le Grice et al. J Virol. 1991 Dec.

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.

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