Abstract
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.