| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 24252 | Journal of Biotechnology | 2009 | 4 Pages |
Abstract
An enzyme-responsive artificial chaperone system which employs an amphiphilic amylose primer (dodecyl maltopentaose, C12-MP) as a surfactant and phosphorylase b was designed to enable protein refolding. Effective refolding of carbonic anhydrase B after both heat denaturation (70 °C for 10 min) and guanidine hydrochloride (6 M) denaturation was observed by controlled association between the protein molecules and the C12-MP primer micelle through an enzymatic reaction.
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Physical Sciences and Engineering
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Bioengineering
Authors
Nobuyuki Morimoto, Naruhito Ogino, Tadashi Narita, Kazunari Akiyoshi,