ArticleBMC biotechnology2015
High-level expression, purification, and enzymatic characterization of truncated human plasminogen (Lys531-Asn791) in the methylotrophic yeast Pichia pastoris.
Article in BMC biotechnology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Scalable secretory production of influenza A (H1N1) hemagglutinin HA1 in Pichia pastoris through expression and process optimization.Microbial cell factories · 2026Article
- Two-sample Mendelian randomization analysis of the causal association between circulating inflammatory proteins and osteosarcoma.Discover oncology · 2025Article
- High expression of antimicrobial peptides cathelicidin-BF inFrontiers in microbiology · 2023Article
- Assessment ofAdvanced pharmaceutical bulletin · 2021Article
- Mutational Analysis of Ocriplasmin to Reduce Proteolytic and Autolytic Activity in Pichia pastoris.Biological procedures online · 2020Article
- A eukaryotic expression strategy for producing the novel antimicrobial peptide PRW4.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2020Article
- Active Expression of Human Tissue Plasminogen Activator (t-PA) c-DNA from Pulmonary Metastases in the Methylotrophic Yeast Pichia Pastoris KM71H StrainAsian Pacific journal of cancer prevention : APJCP · 2017Article
- Expression and characterization of a Talaromyces marneffei active phospholipase B expressed in a Pichia pastoris expression system.Emerging microbes & infections · 2016Article
- In vitro fibrinolysis and antithrombosis characterizations of novel recombinant microplasminogen with RGD and GPRP peptides.Journal of thrombosis and thrombolysis · 2016Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundPlasmin is a serine protease that plays a critical role in fibrinolysis, which is a process that prevents blood clots from growing and becoming problematic. Recombinant human microplasminogen (rhμPlg) is a derivative of plasmin that solely consists of the catalytic domain of human plasmin and lacks the five kringle domains found in the native protein. Developing an industrial production method that provides high yields of this protein with high purity, quality, and potency is critical for preclinical research.
resultsThe human microplasminogen gene was cloned into the pPIC9K vector, and the recombinant plasmid was transformed into Pichia pastoris strain GS115. The concentration of plasmin reached 510.1 mg/L of culture medium. Under fermentation conditions, the yield of rhμPlg was 1.0 g/L. We purified rhμPlg to 96% purity by gel-filtration and cation-exchange chromatography. The specific activity of rhμPlg reached 23.6 U/mg. The K m of substrate hydrolysis by recombinant human microplasmin was comparable to that of human plasmin, while rhμPlm had higher k cat /Km values than plasmin. The high purity and activity of the rhμPlg obtained here will likely prove to be a valuable tool for studies of its application in thrombotic diseases and vitreoretinopathies.
conclusionsReliable rhμPlg production (for use in therapeutic applications) is feasible using genetically modified P. pastoris as a host strain. The successful expression of rhμPlg in P. pastoris lays a solid foundation for its downstream application.
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