Table 1. Comparison of the Apparent k cat and K D Values For PCNA of Pol δ Assembliesa.
| Polymerase Activity | |||
| Pol δ assemblies | k cat (min−1) | Relative k cat | PCNA (K d, nM trimer) |
| Pol δ4 | 77±2.5 | 100 | 7.1±1.0 |
| core+p12 | 83±2.6 | 109 | 8.7±1.2 |
| core+p68 | 31±1.5 | 40 | 9.3±1.9 |
| core | 22±2.7 | 29 | 73±23 |
| p125 | ⋅⋅⋅ | ⋅⋅⋅ | ⋅⋅⋅ |
a
Data from the assays of Pol δ complexes on poly(dA)/oligo(dT) template/primers shown in Figure 1C were fitted into the hyperbola binding equation, v = v basal+{Vmax•[PCNA]/(K d+[PCNA])} where v is the velocity for dNMP incorporation; v basal is the dNMP incorporation without PCNA; K d is the apparent dissociation constant of PCNA. The apparent k cat was calculated as V max/E. The relative specific activities (relative k cat) were determined by taking Pol δ4 as 100.