Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Krause M,Rudolph R,Schwarz Edoi
10.1016/s0014-5793(02)03689-xkeywords:
subject
Has Abstractpub_date
2002-12-04 00:00:00pages
253-5issue
1-2eissn
0014-5793issn
1873-3468pii
S001457930203689Xjournal_volume
532pub_type
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