Figure 2

(A). Self aggregation of sHsp18. sHsp18 protein was purified by denaturing method and dialyzed against 50 mM PBS containing 200 mM NaCl for 12 hrs. Dialyzed protein was precipitated by acetone precipitation. The protein was dissolved in 1.5 M urea and applied to the column equilibrated against PBS and eluted the fractions in PBS. The bands corresponding to oligomeric forms were indicated by dotted arrows and position of molecular weight markers are indicated with solid arrows. (B). Non-denaturing Gel analysis of MagneHis Purified sHsp18 protein. Confirmation of the oligomeric form was done by native gel electrophoresis. Lanes represent High Molecular weight marker (lane 1), 10 μg of Non-denatured BSA showing oligomers (lane 2), 5 and 10 μg of purified protein under non-denatured condition (lanes 3–4), 5 and 10 μg of purified protein under denatured condition (lanes 5–6).