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.