Expression, Purification, and Stability Study of Uricase in Escherichia 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.

Daneshjoo S.; Dashtban Moghadam E.S.; JAAFARI M.R.; Rezayat sorkhabadi S.M.; KHAJEH KH.

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

Journal Paper

Paper Information

Journal: JOURNAL OF BIOTECHNOLOGY Year:2019 | Volume:10 | Issue:2 Page(s): 305-311

Download Full-Text

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

Persian Verion

View:

436

Download:

Cites:

Information Journal Paper

Title

Expression, Purification, and Stability Study of Uricase in Escherichia coli

Author(s)

Keywords

UricaseQ1

RasburicaseQ1

GoutQ1

Uric AcidQ1

Thermal StabilityQ1

Abstract

Some diseases such as Gout, the formation of kidney stones, Lesch-Nyhan syndrome, Heart disease, diabetes type II and metabolic syndrome are caused due to the high concentration of Uric Acid. Within drugs, Uricase significantly decreases the level of Uric Acid in plasma. The production, formulation and preservation proteins need special conditions so that there was no alteration in their structure and highest activity and response, at the same time the lowest immunogenicity can be achieved. In this study, Uricase from Aspergillus flavus was cloned and expressed in Escherichia coli BL21. The protein was then purified using affinity chromatography. The enzyme activity and stability were compared with the common industrial RasbUricase. Results showed higher activity and stability at different temperatures (50, 37, 25, 4, and-20° C). Since Uricase has an important role in the prevention and cure of mentioned diseases, therefore, the stable form of this enzyme could be a potential candidate for drug development.

Cites

No record.

References

No record.

Cite

APA: Copy

Daneshjoo, S., Dashtban Moghadam, E.S., JAAFARI, M.R., Rezayat sorkhabadi, S.M., & KHAJEH, KH.. (2019). Expression, Purification, and Stability Study of Uricase in Escherichia coli. JOURNAL OF BIOTECHNOLOGY, 10(2 ), 305-311. SID. https://sid.ir/paper/231223/en

Vancouver: Copy

Daneshjoo S., Dashtban Moghadam E.S., JAAFARI M.R., Rezayat sorkhabadi S.M., KHAJEH KH.. Expression, Purification, and Stability Study of Uricase in Escherichia coli. JOURNAL OF BIOTECHNOLOGY[Internet]. 2019;10(2 ):305-311. Available from: https://sid.ir/paper/231223/en

IEEE: Copy

S. Daneshjoo, E.S. Dashtban Moghadam, M.R. JAAFARI, S.M. Rezayat sorkhabadi, and KH. KHAJEH, “Expression, Purification, and Stability Study of Uricase in Escherichia coli,” JOURNAL OF BIOTECHNOLOGY, vol. 10, no. 2 , pp. 305–311, 2019, [Online]. Available: https://sid.ir/paper/231223/en

Related Journal Papers