Fig 1. Size exclusion chromatography profile of cupincin on sephadex G 150 column.

(o-o) protein content (*-*) protease activity. The column was pre equilibrated with 50mM Tris-HCl buffer, pH 7.5. A flow rate of 1mL/10 min was set. Fractions were detected at 280 nm. Peak II being highest in terms of proteolytic activity is pooled, concentrated and used for further experiments as described in the materials and methods section. Denatured haemoglobin was used as substrate for activity measurements.