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Title 

A fusion protein expression analysis using surface plasmon resonance imaging

Authors 

Jin Mi JungYong Beom ShinMin-Gon KimHyeon Su RoH T JungBong Hyun Chung

Publisher 

Elsevier

Issue Date 

2004

Citation 

Analytical Biochemistry, vol. 330, no. 2, pp. 251-256

Keywords 

afinity-tagged proteinexpression analysisgold chipsurface plasmon resonance (SPR) imagingdextranglutathioneglutathione transferasehistidine derivativehuman growth hormonehybrid protein

Abstract 

A surface plasmon resonance (SPR) imaging system was constructed and used to detect the affinity-tagged recombinant proteins expressed in Escherichia coli. With regards to model proteins, the hexahistidine-ubiquitin-tagged human growth hormone (His6-Ub-hGH), glutathione S-transferase-tagged human interleukin-6 (GST-hIL6), and maltose-binding protein-tagged human interleukin-6 (MBP-hIL6) expressed in E. coli were analyzed. The cell lysates were spotted on gold thin films coated with 11-mercaptoundecanol (MUOH)/dextran derivatized with Ni(II)-iminodiacetic acid (IDA-Ni(II)), glutathione, or cyclodextrin. After a brief washing of the gold chip, SPR imaging measurements were carried out in order to detect the bound affinity-tagged fusion proteins. Using this new approach, rapid high-throughput expression analysis of the affinity-tagged proteins were obtained. The SPR imaging protein chip system used to measure the expression of affinity-tagged proteins in a high-throughput manner is expected to be an attractive alternative to traditional laborious and time-consuming methods, such as SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and Western blots.

ISSN 

0003-2697

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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