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Immobilized Triton X-100-assisted refolding of Green Fluorescent Protein-Tobacco Etch Virus protease fusion protein using β-cyclodextrin as the eluent

Li, Jing-Jing (author)
Wang, Ai-Qing (author)
Janson, Jan-Christer (author)
Uppsala universitet,Institutionen för fysikalisk och analytisk kemi,Ytbioteknik
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Ballagi, Andras (author)
Uppsala universitet,Ytbioteknik
Chen, Jing (author)
Liu, Yong-Dong (author)
Ma, Guang-Hui (author)
Su, Zhi-Guo (author)
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 (creator_code:org_t)
Elsevier BV, 2009
2009
English.
In: Process Biochemistry. - : Elsevier BV. - 1359-5113 .- 1873-3298. ; 44:3, s. 277-282
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • A new protein refolding technique based on the use of the non-charged detergent Triton X-100 immobilized to the cross-linked agarose gel Sepharose High Performance has been developed. The new solid phase was used in combination with soluble β-cyclodextrin (β-CD) to refold recombinant Green Fluorescent Protein fused to Tobacco Etch Virus protease (GFPTEVP) expressed as inclusion bodies in E. coli. Previous attempts to refold recombinant GFPTEVP by dilution had failed. In the new procedure a column packed with Triton X-100-coupled Sepharose High Performance was used to capture unfolded GFPTEVP followed by elution using an increasing β-CD concentration gradient. The yield of properly refolded GFPTEVP was 46% at a protein concentration of 380 μg/ml. In contrast, dilution refolding of GFPTEVP at 200 μg/ml refolding buffer resulted in only 4.7% of native protein.

Subject headings

NATURVETENSKAP  -- Kemi (hsv//swe)
NATURAL SCIENCES  -- Chemical Sciences (hsv//eng)

Keyword

Immobilized Triton X-100
Sepharose High Performance
Refolding
Green Fluorescent Protein
Hydrophobic interaction chromatography
Artificial chaperone
β-Cyclodextrin
Chemistry
Kemi

Publication and Content Type

ref (subject category)
art (subject category)

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