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Title 

Purification and structural analysis of the hepatitis B virus PreS1 expressed from Escherichia coli

Authors 

Cheol Young MaengMee Sook OhIl Hyun ParkHyo Jeong Hong

Publisher 

Elsevier

Issue Date 

2001

Citation 

Biochemical and Biophysical Research Communications, vol. 282, no. 3, pp. 787-792

Keywords 

hepatitis B virussurface antigenpreS1purificationcircular dichroismsecondary structure

Abstract 

The preS1 of hepatitis B virus (HBV) is located at the outermost part of the envelope protein and possesses several functionally important regions such as hepatocyte receptor-binding site and virus-neutralizing epitopes. As the first step to understand the structure-function relationship for the preS1 antigen, we have purified the preS1 and performed its structural characterization by circular dichroism (CD) spectroscopy. The preS1 was purified to near homogeneity from bacterially expressed glutathione S-transferase (GST)-preS1 fusion protein by two-step purification, affinity chromatography on glutathione-agarose column, and cation-exchange chromatography on Mono S column. The CD analysis showed that the purified preS1, which was largely unstructured in aqueous solution, acquired a significant (16%) α-helical structure when analyzed in 50% trifluoroethanol or 20 mM SDS. The results suggest that the preS1 assumes a mainly unstructured conformation and may form induced secondary structures upon binding to target proteins or under hydrophobic environment.

ISSN 

0006-291X

Link 

http://dx.doi.org/10.1006/bbrc.2001.4641

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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