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. 2013 Jan;87(2):1232–1241. doi: 10.1128/JVI.02441-12

Table 1.

Estimates of dissociation constants for the oligomerization of Rep68* at various concentrations and in the presence of 1 mM ATP or ADPc

Protein and concna (μM) Kd (μM)
K2→1 K4→2 K8→4 K16→8
Apo-Rep68*
    1.0 NDb ND ND ND
    2.1 1.5 1.79 0.16 ND
    4.8 3.26 1.71 0.15 ND
    9.3 2.35 1.98 0.17 1.6
    18.2 1.56 2.56 0.38 0.48
        Avg 2.2 2.0 0.21 1.0
Apo-Rep68* with ATP
    0.7 4.9 NDb ND ND
    1.8 2.0 0.43 0.04 0.16
    4.2 0.75 0.9 0.13 ND
    8.6 0.87 1.26 0.09 0.31
    17 0.96 1.1 0.06 0.07
        Avg 1.9 0.9 0.08 0.18
Apo-Rep68* with ADP
    0.9 0.9 1.1 0.02 ND
    2.1 1.3 0.5 0.04 0.5
    4.2 0.7 0.6 0.05 0.4
    8.8 0.9 ND ND 0.7
    18.1 1.9 1.0 0.05 0.5
        Avg 1.1 0.8 0.04 0.5
a

Total concentration of the Rep68* monomers in the cell obtained from the integration of the complete c(S) distribution from the interference data.

b

ND, not determined.

c

The ∼0.1-fold change in K8→4 relative to that for K4→2 might indicate a entropic effect caused by ring closure. Note also that there seems to be a general small decrease in the values of the dissociation constants when either ATP or ADP is added; although the effect is not large, the trend seems to be there.