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Title 

Efficient expression, purification and characterization of hepatitis B virus preS1 protein from Escherichia coli

Authors 

Hee Sun KimHyo Jeong Hong

Publisher 

Springer Verlag (Germany)

Issue Date 

1995

Citation 

Biotechnology Letters, vol. 17, no. 8, pp. 871-876

Keywords 

cell proteinhybrid proteinvirus proteinbinding siteescherichia coligene expressionhepatitis b virusprotein degradationprotein purification

Abstract 

The complete (encoding 119 aminon acids, aa) or partial (encoding the N-terminal 90 aa) preS1 region gene of hepatitis B virus (HBV) was fused to the 3'-end of glutathione-S-transferase (GST) gene and expressed at 37°C under the control of the inducible tac promoter in E. coli. The results showed that the fusion protein with the full length of preS1 was moderately expressed, about 10% of total cellular proteins, while the protein with the partial preS1 was highly expressed, about 33% of total cellular proteins but the half was degraded into the protein with about N-terminal 60 aa of preS1. Accordingly, GST fusion protein containing the N-terminal 56 aa of the preS1, which still encodes B- and T-cell epitopes and a hepatocyte receptor binding site, was expressed under the same induction conditions and was shown to be highly and stably expressed, about 37% of total cellular proteins. The fusion protein with the full length or N-terminal 56 aa of preS1 and the peptides were simply and successfully purified by affinity chromatography and were demonstrated to exhibit the antigenicity and immunogenicity of the preS1 antigen.

ISSN 

0141-5492

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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