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. 1998 Oct 13;95(21):12135–12140. doi: 10.1073/pnas.95.21.12135

Table 2.

Specificity of ATP-dependent substrate translocation from ClpA to chemically inactivated ClpP

Experiment Additions to first reaction RepA associated with ClpP immunoprecipitates, pmol
1 Complete: [3H]RepA, ClpA, ClpP (inactivated), ATP[γ-S] 1.09 ± 0.11
2 Complete plus 20-fold molar excess of RepA to [3H]RepA 0.05 ± 0.03
3 Complete plus 20-fold molar excess of casein to [3H]RepA 0.17 ± 0.01
4 Complete plus 20-fold molar excess of lysozyme to [3H]RepA 1.09 ± 0.24
5 Complete plus 20-fold molar excess of ovalbumin to [3H]RepA 0.87 ± 0.01
6 Complete, with a 20-fold molar excess of RepA to [3H]RepA added after incubation with ATP 1.14 ± 0.22

Translocation experiments were identical to those described in Fig. 4, but for experiments 2–5 a 20-fold molar excess of unlabeled RepA, α-casein, lysozyme, or ovalbumin was added during the first incubation step as indicated. In experiment 6, a 20-fold molar excess of unlabeled RepA was added after the ATP incubation step. Results are means (±SEM) of two independent experiments.