A fusion protein expression analysis using surface plasmon resonance imaging

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Title
A fusion protein expression analysis using surface plasmon resonance imaging
Author(s)
Jin Mi Jung; Yong Beom Shin; Min-Gon Kim; Hyeon Su Ro; H T Jung; Bong Hyun Chung
Bibliographic Citation
Analytical Biochemistry, vol. 330, no. 2, pp. 251-256
Publication Year
2004
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.
Keyword
Affinity-tagged proteinExpression analysisGold chipSurface plasmon resonance (SPR) imaging
ISSN
0003-2697
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/j.ab.2004.02.009
Type
Article
Appears in Collections:
Division of Research on National Challenges > Bionanotechnology Research Center > 1. Journal Articles
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