Abstract:
: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_name
FEBS Lettjournal_title
FEBS lettersauthors
Stammers DK,Tisdale M,Court S,Parmar V,Bradley C,Ross CKdoi
10.1016/0014-5793(91)80613-8subject
Has Abstractpub_date
1991-06-03 00:00:00pages
298-302issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(91)80613-8journal_volume
283pub_type
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