Linked Life Data

19428720

Source:http://linkedlifedata.com/resource/pubmed/id/19428720

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3-4
pubmed:dateCreated
2009-5-11
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1873-4863
pubmed:author
pubmed:issnType
Electronic
pubmed:day
25
pubmed:volume
140
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
246-9
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Enzyme-responsive artificial chaperone system with amphiphilic amylose primer.
pubmed:affiliation
Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University, 2-3-10 Kanda-Surugadai, Chiyoda-ku, Tokyo 101-0062, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't