Ionic surfactants are used in polyacrylamide gel electrophoresis (PAGE) protein separations, as protein denaturing and solubilizing agents.  Here in, we discuss a cationic ionic liquid (IL) surfactant that can bind and denature proteins to produce cationic IL-protein complexes. In PAGE, these complexes are migrated from anode to cathode. Hence, this technique is known as cationic IL- PAGE. At the optimum conditions, all proteins were separated as sharp bands, with good resolution, and reflective of the molecular weight of proteins. Ribonuclease b (rib b), a glycoprotein, was analyzed by use of cationic IL-PAGE. The electropherogram of rib b showed multiple protein bands with two distinct bands. The two protein bands were further analyzed by protein extraction followed by matrix assisted laser desorption ionization (MALDI)-mass spectrometry (MS). Protein masses were found to be identical with two of the rib b glycoforms, which confirms the separation of rib b glycoforms by one-step cationic IL-PAGE. The same analysis was performed and compared with conventional cationic (cetyltrimethylammonium bromide) CTAB-PAGE and anionic (sodium dodecylsulfate) SDS-PAGE techniques. A single protein band of rib b with a ‘gel shift’ <i>i.e.</i> protein migration is not according to the molecular weight, was observed with both conventional techniques. This could be due to charge heterogeneity of rib b glycoprotein which is compatible with IL-PAGE, but not with CTAB or SDS-PAGE.<br/>

Ionic liquid surfactants in cationic polyacrylamide gel electrophoresis protein separation

253rd National Meeting (2017)

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