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PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2002-12-2
pubmed:abstractText
The non-ionic detergent Brij 58P is recommended as a stabilizing agent for protein storage; for example, the aggregation-prone chaperone DnaJ can be maintained in solution by low concentrations of Brij 58P. During protein folding studies with alpha-glucosidase, rhodanese and citrate synthase as model proteins, we discovered that the low concentrations of Brij 58P usually added with purified DnaJ to renaturation samples are sufficient to mimic chaperone effects with respect to prevention of protein aggregation. Furthermore, addition of Brij 58P to refolding alpha-glucosidase and citrate synthase enhanced the yield of refolded protein by a factor of two. Thus, Brij 58P can mimic chaperone effects and care should be taken when the substance is used to stabilize chaperone preparations.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:author
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
253-5
pubmed:dateRevised
2006-11-15
pubmed:articleTitle
The non-ionic detergent Brij 58P mimics chaperone effects.
pubmed:affiliation
Institute for Biotechnology, Martin-Luther-Universität Halle-Wittenberg, Kurt-Mothes-Strasse 3, 06120 Halle, Germany.