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Title 

Overexpression and simple purification of a truncated, immunologically reactive GST-HCV core (1-123) fusion protein

Authors 

Young Rim SeongEun Kyung LeeSee Young ChoiSeung Ki ChonDong Soo Im

Publisher 

Elsevier

Issue Date 

1996

Citation 

Journal of Virological Methods, vol. 59, no. 1, pp. 13-21

Keywords 

Core proteinHepatitis C virusPurificationcore proteinhybrid proteinamino acid compositionantibody productioncarboxy terminal sequencegenetic linkagehepatitis c virus

Abstract 

A full-length and a truncated gene for the core protein of hepatitis C virus (HCV) were linked to the gene for glutathione S-transferase (GST), and the expression of each GST-HCV core fusion protein was analyzed. The truncated GST-HCV core (1-123) fusion protein was expressed as a mostly soluble and partly insoluble form comprising more than 50% of the total protein in Escherichia coli after induction by isopropylthio-β-D-galactoside (IPTG), while the full length GST-HCV core (1-191) fusion protein was not expressed, suggesting that the hydrophobic carboxy terminal region in the core protein affects its expression. In addition, the GST-HCV core (1-123) fusion protein purified by GST-agarose chromatography reacted specifically with an anti-HCV serum from a patient.

ISSN 

0166-0934

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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