Bordier C
J Biol Chem. 1981 Feb 25;256(4):1604-7.
A solution of the nonionic detergent Triton X-114 is homogeneous at 0 degrees C but separates in an aqueous phase and a detergent phase above 20 degrees C. The extent of this detergent phase separation increases with the temperature and is sensitive to the presence of other surfactants. The partition of proteins during phase separation in solutions of Triton X-114 is investigated. Hydrophilic proteins are found exclusively in the aqueous phase, and integral membrane proteins with an amphiphilic nature are recovered in the detergent phase. Triton X-114 is used to solubilize membranes and whole cells, and the soluble material is submitted to phase separation. Integral membrane proteins can thus be separated from hydrophilic proteins and identified as such in crude membrane or cellular detergent extracts.
非离子去污剂Triton X-114的溶液在0℃时是均匀的，但在20℃以上会分离成水相和去污剂相。这种去污剂相分离的程度随温度升高而增加，并且对其他表面活性剂的存在敏感。研究了Triton X-114溶液相分离过程中蛋白质的分配情况。发现亲水性蛋白质仅存在于水相中，而具有两亲性质的整合膜蛋白则存在于去污剂相中。Triton X-114用于溶解膜和全细胞，然后将可溶性物质进行相分离。因此，整合膜蛋白可以与亲水性蛋白质分离，并在粗膜或细胞去污剂提取物中得以鉴定。
