PURIFICATION AND CHARACTERIZATION OF RECOMBINANT EQUINE INFECTIOUS-ANEMIA VIRUS REVERSE-TRANSCRIPTASE

被引:17
作者
LEGRICE, SFJ
PANIN, M
KALAYJIAN, RC
RICHTER, NJ
KEITH, G
DARLIX, JL
PAYNE, SL
机构
[1] CASE WESTERN RESERVE UNIV, SCH MED, DEPT MOLEC BIOL & MICROBIOL, CLEVELAND, OH 44106 USA
[2] ECOLE NORMALE SUPER LYON, BIOL MOLEC & CELLULAIRE LAB, F-69364 Lyon, FRANCE
[3] INST BIOL MOLEC & CELLULAIRE, F-67084 STRASBOURG, FRANCE
关键词
D O I
10.1128/JVI.65.12.7004-7007.1991
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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, tRNA3Lys 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.
引用
收藏
页码:7004 / 7007
页数:4
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