Production of Mutant Streptokinase Recombinant Protein
| Author | Negar Seyed | en |
| Author | Parvaneh Shekari | en |
| Author | Mojgan Bandehpour | en |
| Author | Zarrin Sharifnia | en |
| Author | Kazem Parivar | en |
| Author | Bahram Kazemi | en |
| Orcid | Bahram Kazemi [0000-0002-3072-8831] | en |
| Issued Date | 2008-10-31 | en |
| Abstract | Background: Streptokinase (SK) is most widely used for treatment of myocardial infarction, however, it is the most expensive thrombolytic agent. A major drawback to SK use is the widespread presence of antistreptokinase antibodies (Abs). These Abs cause allergic reactions and neutralize streptokinase therapeutic effects. Materials and methods: To produce an engineered variant of streptokinase being functional and less antigenic than the native molecule, we cloned and expressed streptokinase mutant gene lacking the C terminal 42 amino acids. Recombinant protein was confirmed by western blot analysis with anti T7 monoclonal antibodies. Results: pGEMEX-1 expression vector contains T7 gene 10 protein as fusion protein immediately down stream of T7 promoter and before multiple cloning site, streptokinase mutant gene was cloned after fusion protein. Conclusion: We cloned and expressed mutant streptokinase gene, lacking the C-terminal 42 amino acids. If mut-C42 activity was less affected by neutralizing antibodies compared with native streptokinase, this engineered variant could be a preferred alternative to native streptokinase for thrombolytic therapy. | en |
| DOI | https://doi.org/ | en |
| Keyword | Streptokinase | en |
| Keyword | Myocardial infarction. Mutation | en |
| Keyword | Cloning | en |
| Publisher | Brieflands | en |
| Title | Production of Mutant Streptokinase Recombinant Protein | en |
| Type | Research Article | en |
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