IMPROVEMENT OF RECOMBINANT STREPTOKINASE PRODUCTION IN E.COLI

Q: How can I download an article?

To download an article from SID, first log in to the site, search for the article title, and click on the 'Download Article' option.

Q: How can I download an ISI article?

To download an ISI article on SID, enter the keyword or article title in the search bar, view the relevant results, click on the desired article, and select the 'Download Article' option.

Q: How can I access the SID database?

To access the SID database, visit SID.ir, create an account, and log in to access scientific resources.

Q: Is downloading articles from SID free?

Some articles on SID are available for free, while others require payment. Details are specified on the article's page.

MOLAEE N.; ABTAHI H.

مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Journal Paper

Paper Information

Journal: ARAK MEDICAL UNIVERSITY JOURNAL (AMUJ) Year:2011 | Volume:14 | Issue:4 (57) Page(s): 98-104

Download Full-Text

Persian Verion

View:

1,448

Download:

Cites:

Information Journal Paper

Title

IMPROVEMENT OF RECOMBINANT STREPTOKINASE PRODUCTION IN E.COLI

Author(s)

MOLAEE N. | ABTAHI H. | Issue Writer Certificate

Keywords

GENE EXPRESSIONQ2

GROUP A STREPTOCOCCUSQ2

STREPTOKINASEQ2

Abstract

Background: STREPTOKINASE is one of the antigenic proteins secreted by streptococcus pyogenes. This protein has an important role in bacterial pathogenesis. The aim of this study was to produce recombinant forms of this enzyme so that the product would change in accordance with changes in the media.Materials and Methods: In this experimental study, we amplified the STREPTOKINASE gene by polymerase chain reaction (PCR) method. After extraction, it was sub-cloned to prokaryotic expression vector pET32a. pET32a-Ska was transferred to E.coli BL21-DE3-plySs strain. Protein production was induced by IPTG and optimization of culture media and OD of bacteria. The recombinant protein was extracted by Ni-NTA and its concentration was measured by Bradford assay. Western- Blot analysis was used to verify the recombinant protein.Results: The nucleotide sequence of the amplified gene was the same as STREPTOKINASE gene of the streptococcus pyogenes. The production of recombinant STREPTOKINASE by induction of plasmid pET32a-Ska was done by IPTG. The recombinant STREPTOKINASE had the same antigenic properties as natural STREPTOKINASE. The largest amount of recombinant protein was produced in bacteria concentrations with OD=0.8. Also, the production of the recombinant protein was higher in media with no glucose.Conclusion: Changes in culture media can increase the production of recombinant proteins in host bacteria. The presence of nutrients, such as glucose, alone not only can not increase the amount of production but it might even decrease it.

Cites

No record.

References

No record.

Cite

APA: Copy

MOLAEE, N., & ABTAHI, H.. (2011). IMPROVEMENT OF RECOMBINANT STREPTOKINASE PRODUCTION IN E.COLI. ARAK MEDICAL UNIVERSITY JOURNAL (AMUJ), 14(4 (57)), 98-104. SID. https://sid.ir/paper/69462/en

Vancouver: Copy

MOLAEE N., ABTAHI H.. IMPROVEMENT OF RECOMBINANT STREPTOKINASE PRODUCTION IN E.COLI. ARAK MEDICAL UNIVERSITY JOURNAL (AMUJ)[Internet]. 2011;14(4 (57)):98-104. Available from: https://sid.ir/paper/69462/en

IEEE: Copy

N. MOLAEE, and H. ABTAHI, “IMPROVEMENT OF RECOMBINANT STREPTOKINASE PRODUCTION IN E.COLI,” ARAK MEDICAL UNIVERSITY JOURNAL (AMUJ), vol. 14, no. 4 (57), pp. 98–104, 2011, [Online]. Available: https://sid.ir/paper/69462/en

Related Journal Papers