Krause Matthias, Rudolph Rainer, Schwarz Elisabeth
Institute for Biotechnology, Martin-Luther-Universität Halle-Wittenberg, Kurt-Mothes-Strasse 3, 06120 Halle, Germany.
FEBS Lett. 2002 Dec 4;532(1-2):253-5. doi: 10.1016/s0014-5793(02)03689-x.
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.
非离子型去污剂Brij 58P被推荐作为蛋白质储存的稳定剂;例如,易于聚集的伴侣蛋白DnaJ可以通过低浓度的Brij 58P维持在溶液中。在用α-葡萄糖苷酶、硫氰酸酶和柠檬酸合酶作为模型蛋白进行蛋白质折叠研究时,我们发现通常与纯化的DnaJ一起添加到复性样品中的低浓度Brij 58P足以模拟伴侣蛋白在防止蛋白质聚集方面的作用。此外,向重折叠的α-葡萄糖苷酶和柠檬酸合酶中添加Brij 58P可使重折叠蛋白的产量提高两倍。因此,Brij 58P可以模拟伴侣蛋白的作用,在使用该物质稳定伴侣蛋白制剂时应谨慎。