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The C-termini of p66 and p51 forms of HIV-1 reverse transcriptase have been engineered to contain a Glu-Glu-Phe sequence recognized by a monoclonal antibody to alpha-tubulin, YL1/2. Mutated RTs were purified in a single step using peptide elution from columns of immobilized YL1/2. The known sequence requirements of the YL1/2 epitope are consistent with protein eluting from the column with an intact C-terminus. Kinetic parameters of these mutated RTs are essentially unchanged from wild-type enzyme. The p15 RNaseH domain has been purified using this method and shown to have low enzyme activity compared to the parental p66 subunit.


Journal article



Publication Date





298 - 302


Amino Acid Sequence, Blotting, Western, Chromatography, Affinity, Electrophoresis, Polyacrylamide Gel, Endoribonucleases, Epitopes, Genes, Viral, Genetic Engineering, HIV Protease, HIV-1, Molecular Sequence Data, Molecular Weight, Mutagenesis, Site-Directed, Polymerase Chain Reaction, RNA-Directed DNA Polymerase, Recombinant Proteins, Restriction Mapping, Ribonuclease H, Tubulin, Viral Structural Proteins