Detergent Mediated Effects on the High-Performance Liquid Chromatography of Proteins

摘要

Present chromatographic systems for the high-performance liquid chromatography (HPLC) of hydrophobic-proteins are generally limited to size-exclusion or ion-exchange chromatography. A major stumbling block to the successful chromatography of membrane-proteins is their limited solubility. Detergent is usally required to solublize these proteins. This detergent causes some problems in size-exclusion chromatography, but does not always interfere with the separation. It is more deleterious in anion-exchange chromatography, where ionic detergents can poison the column, and reversed-phase chromatography, where strong interactions can occur between the stationary phase and detergent. Successful chromatography of membrane-proteins requires favorable detergent/stationary-phase interactions that enhance, rather than interfere with, the separation.