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231223s2011 xx |||||o 00| ||eng c |
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|a 10.1021/la1050404
|2 doi
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|a pubmed24n0687.xml
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|e rakwb
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|a eng
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|a Xu, Fei
|e verfasserin
|4 aut
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|a Polymer brush-modified magnetic nanoparticles for His-tagged protein purification
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|c 2011
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|2 rdamedia
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|a ƒa Online-Ressource
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|a Date Completed 21.10.2014
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|a Date Revised 20.10.2021
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Growth of poly(2-hydroxyethyl methacrylate) brushes on magnetic nanoparticles and subsequent brush functionalization with nitrilotriacetate-Ni(2+) yield magnetic beads that selectively capture polyhistidine-tagged (His-tagged) protein directly from cell extracts. Transmission electron microscopy, Fourier transform infrared (FT-IR) spectroscopy, thermogravimetric analysis, and magnetization measurements confirm and quantify the formation of the brushes on magnetic particles, and multilayer protein adsorption to these brushes results in binding capacities (220 mg BSA/g of beads and 245 mg His-tagged ubiquitin/g of beads) that are an order of magnitude greater than those of commercial magnetic beads. Moreover, the functionalized beads selectively capture His-tagged protein within 5 min. The high binding capacity and protein purity along with efficient protein capture in a short incubation time make brush-modified particles attractive for purification of recombinant proteins
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|a Journal Article
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|a Research Support, N.I.H., Extramural
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|a Research Support, U.S. Gov't, Non-P.H.S.
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|a Magnetite Nanoparticles
|2 NLM
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|a Ubiquitin
|2 NLM
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|a Polyhydroxyethyl Methacrylate
|2 NLM
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|a 25249-16-5
|2 NLM
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|a Histidine
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|a 4QD397987E
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|a Geiger, James H
|e verfasserin
|4 aut
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|a Baker, Gregory L
|e verfasserin
|4 aut
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|a Bruening, Merlin L
|e verfasserin
|4 aut
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 27(2011), 6 vom: 15. März, Seite 3106-12
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|x 1520-5827
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|g volume:27
|g year:2011
|g number:6
|g day:15
|g month:03
|g pages:3106-12
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|u http://dx.doi.org/10.1021/la1050404
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