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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.

Type

Journal article

Journal

FEBS Lett

Publication Date

03/06/1991

Volume

283

Pages

298 - 302

Keywords

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