OVEREXPRESSION OF FULL-LENGTH CORE PROTEIN OF HEPATITIS C VIRUS BY ESCHERICHIA COLI CULTIVATED IN STIRRED TANK FERMENTOR

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.

HEMMAT JAFAR; YAKHCHALI BAGHER; KHAJEH KHOSRO; MOOSAVI MOVAHEDI ALI AKBAR; KARKHANE ALI ASGHAR

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

Journal Paper

Paper Information

Journal: Iranian Journal of Biotechnology Year:2011 | Volume:9 | Issue:4 Page(s): 245-252

Download Full-Text

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

Persian Verion

View:

1,002

Download:

194

Cites:

Information Journal Paper

Title

OVEREXPRESSION OF FULL-LENGTH CORE PROTEIN OF HEPATITIS C VIRUS BY ESCHERICHIA COLI CULTIVATED IN STIRRED TANK FERMENTOR

Author(s)

Keywords

HEPATITIS C VIRUSQ3

CORE PROTEINQ2

OVEREXPRESSIONQ2

RECOMBINANT PROTEINQ2

Abstract

The mature CORE PROTEIN of the HEPATITIS C VIRUS (HCVC173) carrying pelB as a signal peptide (PelB: core) was overexpressed in Escherichia coli as 18% and 23.3% of the host’s total protein, in flask and fermentor cultivation, respectively. A final specific yield of 25±1 mg HCVC173/g dry cell weight and an overall productivity of 51±1 mg HCVC173/l/h were obtained in the stirred-tank fermentor. The recombinant PelB:: CORE PROTEIN was overexpressed as the inclusion body (IB) form, higher than the expected level when compared to the HCVC173, which was also showed by the analysis of secondary structure of mRNAs and calculation of the Codon Adaptation Index of the gene.The results showed that the combined effects of protein fusion and the signal sequence significantly enhanced the production of recombinant mature HCVC173 in E. coli. Therefore, the fusion form of the mature HCV CORE PROTEIN and the conditions defined in this study provide an alternative strategy for HCVC173 production in high cell density culture of E. coli.

Cites

No record.

References

No record.

Cite

APA: Copy

HEMMAT, JAFAR, YAKHCHALI, BAGHER, KHAJEH, KHOSRO, MOOSAVI MOVAHEDI, ALI AKBAR, & KARKHANE, ALI ASGHAR. (2011). OVEREXPRESSION OF FULL-LENGTH CORE PROTEIN OF HEPATITIS C VIRUS BY ESCHERICHIA COLI CULTIVATED IN STIRRED TANK FERMENTOR. IRANIAN JOURNAL OF BIOTECHNOLOGY, 9(4), 245-252. SID. https://sid.ir/paper/139337/en

Vancouver: Copy

HEMMAT JAFAR, YAKHCHALI BAGHER, KHAJEH KHOSRO, MOOSAVI MOVAHEDI ALI AKBAR, KARKHANE ALI ASGHAR. OVEREXPRESSION OF FULL-LENGTH CORE PROTEIN OF HEPATITIS C VIRUS BY ESCHERICHIA COLI CULTIVATED IN STIRRED TANK FERMENTOR. IRANIAN JOURNAL OF BIOTECHNOLOGY[Internet]. 2011;9(4):245-252. Available from: https://sid.ir/paper/139337/en

IEEE: Copy

JAFAR HEMMAT, BAGHER YAKHCHALI, KHOSRO KHAJEH, ALI AKBAR MOOSAVI MOVAHEDI, and ALI ASGHAR KARKHANE, “OVEREXPRESSION OF FULL-LENGTH CORE PROTEIN OF HEPATITIS C VIRUS BY ESCHERICHIA COLI CULTIVATED IN STIRRED TANK FERMENTOR,” IRANIAN JOURNAL OF BIOTECHNOLOGY, vol. 9, no. 4, pp. 245–252, 2011, [Online]. Available: https://sid.ir/paper/139337/en

Related Journal Papers