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Integrated strategy for selective expanded bed ion-exchange adsorption and site-specific protein processing using gene fusion technology
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- Gräslund, Torbjörn (author)
- KTH,Biokemi och biokemisk teknologi,Proteinvetenskap
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- Hedhammar, My (author)
- KTH,Biokemi och biokemisk teknologi,Proteinteknologi
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- Uhlén, Mathias (author)
- KTH,Biokemi och biokemisk teknologi,Systembiologi
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- (creator_code:org_t)
- Elsevier BV, 2002
- 2002
- English.
- In: Journal of Biotechnology. - : Elsevier BV. - 0168-1656 .- 1873-4863. ; 96:1, s. 93-102
- Journal article (peer-reviewed)
Abstract
Subject headings
Close
- The highly charged domain Z(basic) can be used as a fusion partner to enhance adsorption of target proteins to cation exchanging resins at high pH-values. In this paper, we describe a strategy for purification of target proteins fused to Z(basic) at a constant physiological pH using cation exchange chromatography in an expanded bed mode. We show that two proteins, Klenow DNA polymerase and the viral protease 3C, can be efficiently purified from unclarified Escherichia coli homogenates in a single step with a selectivity analogous to what is normally achieved by affinity chromatography. The strategy also includes an integrated site-specific removal of the Z(basic) purification handle to yield a free target protein.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Keyword
- protein A
- Z(basic)
- ion-exchange chromatography
- expanded bed adsorption
- DNA-POLYMERASE-I
- ESCHERICHIA-COLI
- PURIFICATION
- RECOVERY
- COXSACKIEVIRUS-B3
- CHROMATOGRAPHY
- EXPRESSION
- EFFICIENT
- CELLS
- Biochemistry
- Biokemi
Publication and Content Type
- ref (subject category)
- art (subject category)
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- Uhlén, Mathias
- Nygren, Per-Åke
- Hober, Sophia
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- NATURAL SCIENCES
- NATURAL SCIENCES
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- Royal Institute of Technology
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