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pubmed-article:19428720pubmed:abstractTextAn 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 degrees C for 10min) and guanidine hydrochloride (6M) denaturation was observed by controlled association between the protein molecules and the C12-MP primer micelle through an enzymatic reaction.lld:pubmed
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pubmed-article:19428720pubmed:year2009lld:pubmed
pubmed-article:19428720pubmed:articleTitleEnzyme-responsive artificial chaperone system with amphiphilic amylose primer.lld:pubmed
pubmed-article:19428720pubmed:affiliationInstitute of Biomaterials and Bioengineering, Tokyo Medical and Dental University, 2-3-10 Kanda-Surugadai, Chiyoda-ku, Tokyo 101-0062, Japan.lld:pubmed
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