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 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.
journal_name
J Biotechnoljournal_title
Journal of biotechnologyauthors
Morimoto N,Ogino N,Narita T,Akiyoshi Kdoi
10.1016/j.jbiotec.2009.01.013subject
Has Abstractpub_date
2009-03-25 00:00:00pages
246-9issue
3-4eissn
0168-1656issn
1873-4863pii
S0168-1656(09)00033-9journal_volume
140pub_type
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journal_title:Journal of biotechnology
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journal_title:Journal of biotechnology
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journal_title:Journal of biotechnology
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