A fusion protein expression analysis using surface plasmon resonance imaging

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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 (His(6)-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. (C) 2004 Elsevier Inc. All rights reserved.
Publisher
Academic Press Inc Elsevier Science
Issue Date
2004-07
Language
English
Article Type
Article
Keywords

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Citation

ANALYTICAL BIOCHEMISTRY, v.330, no.2, pp.251 - 256

ISSN
0003-2697
DOI
10.1016/j.ab.2004.02.009
URI
http://hdl.handle.net/10203/84953
Appears in Collection
CBE-Journal Papers(저널논문)
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