Triton X-114 Phase Partitioning for Antigen Characterization

In 1981, Bordier (1 ) first demonstrated that Triton X-114 could be exploited as a means of separating hydrophilic and integral membrane proteins. Since then, Triton X-114 phase partitioning has been extensively used for identification and isolation of membrane proteins and has proved to be a convenient method for obtaining enriched preparation of membrane proteins that retain biological activity (2 ). By making some modifications to the original methodology, Smythe et al. (3 ) have improved the procedure to make it more suitable for isolation of integral membrane proteins from Plasmodium falciparum-infected human erythrocytes. The technique now has been used in the characterization of several integral membrane proteins of plasmodia species, including MSP2, AMA1, MSP4, and MSP5 (4 -8 ).