Source:http://linkedlifedata.com/resource/pubmed/id/10942288
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-2
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pubmed:dateCreated |
2000-11-28
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pubmed:abstractText |
The function of a stimuli-responsive polymer was studied for the utilization of protein unfolding and refolding in protein separation using aqueous two-phase systems (ATPS). Poly(ethylene glycol) (PEG) bound to a thermo-reactive hydrophobic head (poly(propylene oxide)-phenyl group (PPO-Ph group)) was used as the functional ligand to modify the PEG phase of the aqueous two-phase systems. Firstly, refolding of carbonic anhydrase from bovine (CAB) was examined in the presence of PPO-Ph-PEG at various temperatures. The refolding yield of CAB was strongly enhanced and aggregate formation was suppressed by addition of PPO-Ph-PEG at a specific temperature (50-55 degrees C). The change in the local hydrophobicity of CAB and PPO-Ph-PEG was characterized using the aqueous two-phase partitioning method and a hydrophobic fluorescent probe. The local hydrophobicity of CAB was maximized at 60 degrees C. The local hydrophobicity of PPO-Ph-PEO was also found to be increased above 45 degrees C. A simple model for CAB refolding, which includes (i) PPO-Ph-PEG complex formation and CAB in the intermediate state and (ii) refolding and release of native CAB from the PPO-Ph-PEG surface, is suggested based on the evaluated surface hydrophobicity.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1387-2273
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
743
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
215-23
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:10942288-Animals,
pubmed-meshheading:10942288-Carbonic Anhydrases,
pubmed-meshheading:10942288-Cattle,
pubmed-meshheading:10942288-Hot Temperature,
pubmed-meshheading:10942288-Polyethylene Glycols,
pubmed-meshheading:10942288-Protein Folding,
pubmed-meshheading:10942288-Temperature,
pubmed-meshheading:10942288-Water
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pubmed:year |
2000
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pubmed:articleTitle |
Protein refolding using stimuli-responsive polymer-modified aqueous two-phase systems.
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pubmed:affiliation |
Department of Chemical Science and Engineering, Graduate School of Engineering Science, Osaka University, Toyonaka, Japan. kuboi@cheng.es.osaka-u.ac.jp
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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