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Updated: Jul 18, 2026

Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain
Published on: December 12, 2017
Refolding, purification, and activation of miniplasminogen and microplasminogen isolated from E. coli inclusion
Dan Medynski1, Michael Tuan, Wayne Liu
1Proteomtech Inc., 3505 Cadillac Ave., Building F7, Costa Mesa, CA 92626, USA.
Abstract:
Two des-kringle derivatives of human plasminogen, microplasminogen and miniplasminogen, have been expressed at high levels as inclusion bodies in Escherichia coli using a T7 expression system. In each case, the isolated inclusion bodies were refolded and purified. A final yield of approximately 10% of total refolded protein was observed in each case. Both refolded molecules were successfully activated to their functional forms, microplasmin and miniplasmin, by the plasminogen activator urokinase. The kinetic properties of the refolded microplasmin and miniplasmin were comparable to full length, native plasmin.

