ArticleThe protein journal2012
Construction, expression and refolding of a bifunctional fusion protein consisting of C-terminal 12-residue of hirudin-PA and reteplase.
Article in The protein journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 13 citations in OpenAlex.
- Insights Into The Effects of Amino Acid Substitutions on The Stability of Reteplase Structure: A Molecular Dynamics Simulation Study.Iranian journal of biotechnology · 2023Article
- Pharmacological Activities and Mechanisms of Hirudin and Its Derivatives - A Review.Frontiers in pharmacology · 2021Review
- Reteplase: Structure, Function, and Production.Advanced biomedical research · 2019Review
- Computational design, functional analysis and antigenic epitope estimation of a novel hybrid of 12 peptides of hirudin and reteplase.Journal of molecular modeling · 2015Article
- Molecular cloning of Reteplase and its expression in E. coli using tac promoter.Advanced biomedical research · 2014Article
- Expression of the recombinant plasminogen activator (reteplase) by a non-lytic insect cell expression system.Research in pharmaceutical sciences · 2013Article
- Comparison of Three Escherichia coli Strains in Recombinant Production of Reteplase.Avicenna journal of medical biotechnologyArticle
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To obtain a bifunctional protein simultaneously showing bioactivity of anticoagulant and fibrinolytic for use in the treatment of thrombotic diseases, we constructed a fusion protein (HV12p-rPA) containing C-terminal 12-residue of hirudin-PA (HV12p) and reteplase (rPA). The fusion protein, in which HV12p was linked to rPA via Gly-Gly-Gly, was successfully expressed in an inactive form of inclusion bodies in Escherichia coli. HV12p-rPA was identified by sodium dodecylsulfate-polyacrylamide gel electrophoresis. The expression level of HV12p-rPA was optimized by an orthogonal method and finally enhanced from 12 % to approximate 30 %. We also deeply investigated the condition of renaturation of HV12p-rPA, and the inactive protein was partly renatured through various conditions. The refolding efficacy of HV12p-rPA estimated by the recovery of fibrinolytic activity varied from 0.03 % to 16.6 % and the anticoagulant activity fluctuated in the range from 41 to 2,297 ATU/mg. Bioassays indicated that the resulted fusion protein, as expected, exhibited both fibrinolytic and anticoagulant activities. These works laid a foundation for further characterization of HV12p-rPA.
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