Full Length Research Paper
Abstract
A disintegrin echistatin mutant, R24K-echistatin, was obtained by overlap extension polymerase chain reaction. It was efficiently expressed as a soluble and fusion protein in Escherichia coli at optimized fermentation conditions. The recombinant bacteria had the highest wet weight of 120 g/l in 2´YT medium with IPTG induction. The R24K-echistatin was purified by chitin affinity chromatography and had a yield of 13 mg/l with DTT-cleavage. The purified R24K-echistatin inhibited the aggregation of platelet in vitro with IC50 of 21 nM which is better efficient than echistatin. This work lays the foundation for further research on specific anti-thrombus disintegrin agents.
Key words: Disintegrin, echistatin, Escherichia coli, fermentation, mutant.
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