Phase separation of integral membrane proteins in Triton X-114 solution. Export

@article{citeulike:3179930, abstract = {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.}, author = {Bordier, C.}, citeulike-article-id = {3179930}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/6257680}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=6257680}, day = {25}, issn = {0021-9258}, journal = {The Journal of biological chemistry}, keywords = {triton\_x-114}, month = {February}, number = {4}, pages = {1604--1607}, posted-at = {2008-09-01 22:02:46}, priority = {2}, title = {Phase separation of integral membrane proteins in Triton X-114 solution.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/6257680}, volume = {256}, year = {1981} }

TY - JOUR ID - citeulike:3179930 L3 - citeulike-article-id:3179930 N2 - 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. IS - 4 JF - The Journal of biological chemistry SN - 0021-9258 EP - 1607 TI - Phase separation of integral membrane proteins in Triton X-114 solution. VL - 256 SP - 1604 KW - triton_x-114 AU - Bordier, C PY - 1981/02/25/ UR - http://view.ncbi.nlm.nih.gov/pubmed/6257680 ER -