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| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 03315naa a2200565 4500 | |
| 001 | oai:DiVA.org:kth-13276 | |
| 003 | SwePub | |
| 008 | 100609s2002 | |||||||||||000 ||eng| | |
| 009 | oai:DiVA.org:kth-250622 | |
| 024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-132762 URI |
| 024 | 7 | a https://doi.org/10.1016/S0168-1656(02)00040-82 DOI |
| 024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-2506222 URI |
| 040 | a (SwePub)kth | |
| 041 | a engb eng | |
| 042 | 9 SwePub | |
| 072 | 7 | a ref2 swepub-contenttype |
| 072 | 7 | a art2 swepub-publicationtype |
| 100 | 1 | a Gräslund, Torbjörnu KTH,Biokemi och biokemisk teknologi,Proteinvetenskap4 aut0 (Swepub:kth)u1dl39rj |
| 245 | 1 0 | a Integrated strategy for selective expanded bed ion-exchange adsorption and site-specific protein processing using gene fusion technology |
| 264 | 1 | b Elsevier BV,c 2002 |
| 338 | a print2 rdacarrier | |
| 500 | a QC 20100609 | |
| 500 | a QC 20201020 | |
| 520 | a 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. | |
| 650 | 7 | a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe |
| 650 | 7 | a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng |
| 653 | a protein A | |
| 653 | a Z(basic) | |
| 653 | a ion-exchange chromatography | |
| 653 | a expanded bed adsorption | |
| 653 | a DNA-POLYMERASE-I | |
| 653 | a ESCHERICHIA-COLI | |
| 653 | a PURIFICATION | |
| 653 | a RECOVERY | |
| 653 | a COXSACKIEVIRUS-B3 | |
| 653 | a CHROMATOGRAPHY | |
| 653 | a EXPRESSION | |
| 653 | a EFFICIENT | |
| 653 | a CELLS | |
| 653 | a Biochemistry | |
| 653 | a Biokemi | |
| 700 | 1 | a Hedhammar, Myu KTH,Biokemi och biokemisk teknologi,Proteinteknologi4 aut0 (Swepub:kth)u1o2n86z |
| 700 | 1 | a Uhlén, Mathiasu KTH,Biokemi och biokemisk teknologi,Systembiologi4 aut0 (Swepub:kth)u1dulvmw |
| 700 | 1 | a Nygren, Per-Åkeu KTH,Biokemi och biokemisk teknologi,Albanova VinnExcellence Center for Protein Technology, ProNova4 aut0 (Swepub:kth)u1zhverl |
| 700 | 1 | a Hober, Sophiau KTH,Biokemi och biokemisk teknologi,Science for Life Laboratory, SciLifeLab,Albanova VinnExcellence Center for Protein Technology, ProNova,Proteinteknologi4 aut0 (Swepub:kth)u11qqzc1 |
| 710 | 2 | a KTHb Biokemi och biokemisk teknologi4 org |
| 773 | 0 | t Journal of Biotechnologyd : Elsevier BVg 96:1, s. 93-102q 96:1<93-102x 0168-1656x 1873-4863 |
| 856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-13276 |
| 856 | 4 8 | u https://doi.org/10.1016/S0168-1656(02)00040-8 |
| 856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-250622 |
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