Highly effective renaturation of a streptokinase from Streptococcus pyogenes DT7 as inclusion bodies overexpressed in Escherichia coli.

ABSTRACT: The streptokinase (SK) is emerging as an important thrombolytic therapy agent in the treatment of patients suffering from cardiovascular diseases. We reported highly effective renaturation of a SK from S. pyogeness DT7 overexpressed in E. coli, purification, and biochemical characterization. A gene coding for the SK was cloned from S. pyogeness DT7. Because accumulation of active SK is toxic to the host cells, we have expressed it in the form of inclusion bodies. The mature protein was overexpressed in E. coli BL21 DE3/pESK under the control of the strong promoter tac induced by IPTG with a level of 60% of the total cell proteins. The activity of the rSK, renatured in phosphate buffer supplemented with Triton X-100 and glycerol, was covered with up to 41 folds of its initial activity. The

SUBMITTER: Nguyen Sle T 

PROVIDER: S-EPMC4026873 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature