We have shown that bacteriophage T5-induced DNA polymerase replicates short primer-templates (400 to 600 nucleotides long) at a rapid rate initially, followed by a slower rate sustained for much longer periods (Das, S. K., and Fujimura, R. K. (1977) J. Biol. Chem. 252, 8700-8707). In order to explain the slower steady rate and the results of polymer-challenge experiments, we conjectured the presence of a "dead-end complex" formed by the enzyme with the primer-template at the end of the primer elongation process. In this communication we present evidence which indicates that the presumed complex shows a first order kinetics of decay with a half-life of 3.5 min at 37 degrees. Energies of activation for the steady phase of synthesis and the decay of the dead-end complex were both found to be about 23 kcal/mol. This indicates that the dissociation of the aforesaid complex might be the rate-limiting step during the steady phase of synthesis. Correlation between the salt-induced reduction in the half-life of the complex and the increase in the steady rate of synthesis is in agreement with the above mentioned possibility.