REFOLDING PROCESS OF CYSTEINE-RICH PROTEINS: CHITINASE AS A MODEL

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.

MOGHADAM MALIHEH; GANJI ALI; VARASTEH ABDOLREZA; FALAK REZA; SANKIAN MOJTABA

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

Journal Paper

Paper Information

Journal: REPORTS OF BIOCHEMISTRY AND MOLECULAR BIOLOGY Year:2015 | Volume:4 | Issue:1 Page(s): 0-0

Download Full-Text

View:

352

Download:

163

Cites:

Information Journal Paper

Title

REFOLDING PROCESS OF CYSTEINE-RICH PROTEINS: CHITINASE AS A MODEL

Author(s)

Keywords

CHITINASE

CYSTEINE-RICH PROTEINS

PROTEIN REFOLDING

PROTEIN SOLUBILIZATION

Abstract

Background: Recombinant proteins overexpressed in E. coli are usually deposited in inclusion bodies. Cysteines in the protein contribute to this process. Inter- and intra-molecular disulfide bonds in CHITINASE, a cysteine-rich protein, cause aggregation when the recombinant protein is overexpressed inE. coli. Hence, aggregated proteins should be solubilized and allowed to refold to obtain native- or correctly- folded recombinant proteins.Methods: Dilution method that allows refolding of recombinant proteins, especially at high protein concentrations, is to slowly add the soluble protein to refolding buffer. For this purpose: first, the inclusion bodies containing insoluble proteins were purified; second, the aggregated proteins were solubilized; finally, the soluble proteins were refolded using glutathione redox system, guanidinium chloride, dithiothreitol, sucrose, and glycerol, simultaneously.Results: After PROTEIN SOLUBILIZATION and refolding, SDS-PAGE showed a 32 kDa band that was recognized by an anti-chitin antibody on western blots.Conclusion: By this method, CYSTEINE-RICH PROTEINS from E. coli inclusion bodies can be solubilized and correctly folded into active proteins.

Multimedia

No record.

Cites

No record.

References

No record.

Cite

APA: Copy

MOGHADAM, MALIHEH, GANJI, ALI, VARASTEH, ABDOLREZA, FALAK, REZA, & SANKIAN, MOJTABA. (2015). REFOLDING PROCESS OF CYSTEINE-RICH PROTEINS: CHITINASE AS A MODEL. REPORTS OF BIOCHEMISTRY AND MOLECULAR BIOLOGY, 4(1), 0-0. SID. https://sid.ir/paper/343094/en

Vancouver: Copy

MOGHADAM MALIHEH, GANJI ALI, VARASTEH ABDOLREZA, FALAK REZA, SANKIAN MOJTABA. REFOLDING PROCESS OF CYSTEINE-RICH PROTEINS: CHITINASE AS A MODEL. REPORTS OF BIOCHEMISTRY AND MOLECULAR BIOLOGY[Internet]. 2015;4(1):0-0. Available from: https://sid.ir/paper/343094/en

IEEE: Copy

MALIHEH MOGHADAM, ALI GANJI, ABDOLREZA VARASTEH, REZA FALAK, and MOJTABA SANKIAN, “REFOLDING PROCESS OF CYSTEINE-RICH PROTEINS: CHITINASE AS A MODEL,” REPORTS OF BIOCHEMISTRY AND MOLECULAR BIOLOGY, vol. 4, no. 1, pp. 0–0, 2015, [Online]. Available: https://sid.ir/paper/343094/en

Related Journal Papers

No record.

Related Seminar Papers

No record.

Related Plans

No record.

Recommended Workshops