Refolding activity in the presence of increasing concentrations of wild-type and low-affinity co-chaperonins.

<p>Refolding of 0.33 µM HCl-denatured MDH by 10 µM of chaperonin GroEL (A), wild-type mHsp60 (B), E321K mHsp60 (C), R264K/E358K mHsp60 (D), in the presence of increasing concentrations of mHsp10 (white triangles), GroES (black triangles) and the low-affinity mutants: mHsp10_L33A (white diamonds) and GroES_L27A (black diamonds). MDH activity was measured at 340 nm following 120 min incubation at 30°C in the presence of 1 mM ATP. The 100% reference was determined as the activity of a sample containing the same amount of native MDH.