Investigating the Chaperone Properties of a Novel Heat Shock Protein, Hsp70.c, from Trypanosoma brucei
Figure 5
Stimulation of TbHsp70.c and TcHsp70B ATPase activity by co-chaperone Tbj2. The ATPase activity of TbHsp70.c (0.4 µM) and TcHsp70B (0.4 µM) was assayed in the absence and presence of Tbj2 at equimolar concentrations. Tbj2 was assayed in a 2-fold molar excess to TbHsp70.c (1 µM) and TcHsp70B (1 µM). The unstimulated ATPase activity of TbHsp70.c and TcHsp70B is represented by 100%. The concentration of ATP, present in all reactions, was maintained at 600 µM. The data points were determined from triplicate ATPase activity measurements for three independent batches of purified protein and the data shown represents that of a typical experiment. The bars represent standard deviations. and .
