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A higher affinity of AMV reverse transcriptase for template‐primers correlates with a lower rate of DNA synthesis
Author(s) -
Parnaik Veena K.,
Das M.R.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80748-0
Subject(s) - primer (cosmetics) , reverse transcriptase , microbiology and biotechnology , enzyme , primer binding site , chemistry , dna , kinetics , dna polymerase , biochemistry , biology , polymerase chain reaction , physics , organic chemistry , quantum mechanics , gene
The kinetics of copying of poly (A)‐oligo (dT) and poly (C)‐oligo (dG) by reverse transcriptase from avian myeloblastosis virus have been studied, and binding affinity of enzyme for template‐primer and primer alone have been determined separately. Although the maximal rate of DNA synthesis obtained with poly (C)‐oligo (dG) is higher than that for poly (A)‐oligo (dT), the binding affinity of the enzyme for poly (C)‐oligo (dG) or oligo (dG) is considerably lower than that for poly (A)‐oligo (dT) or oligo (dT). Hence, for the more efficient template, poly (C)‐oligo (dG), both template‐primer and primer bind less tightly to the enzyme.