A higher affinity of AMV reverse transcriptase for template-primers correlates with a lower rate of DNA synthesis.
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.
D001354:Avian Leukosis Virus / Q000201:enzymology*; D009189:Avian Myeloblastosis Virus / Q000201:enzymology*; D004261:DNA Replication; D007700:Kinetics; D012194:RNA-Directed DNA Polymerase / Q000378:metabolism*; D013329:Structure-Activity Relationship; D013698:Templates, Genetic
D012194:RNA-Directed DNA Polymerase