The non‐ionic detergent Brij 58P mimics chaperone effects

FEBS Letters

Krause, Matthias¹  Rudolph, Rainer¹  Schwarz, Elisabeth¹ 

[1]Institute for Biotechnology, Martin-Luther-Universität Halle–Wittenberg, Kurt-Mothes-Strasse 3, 06120 Halle, Germany

关键词: Brij 58P;    Chaperone;    Protein aggregation;    Protein folding;   

DOI  :  10.1016/S0014-5793(02)03689-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 α-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 α-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.

【 授权许可】

Unknown