Abstract
The addition of the sodium salt of phytic acid to the separation buffer (pH's 6.0-9.5) has allowed the analysis of a number of basic proteins (pI's > 9) by capillary electrophoresis. The method of analysis is simple and leads to considerable improvement in peak shape. Some very basic proteins, totally adsorbed onto the capillary fused silica surfaces in the presence of buffer only, can be analysed as sharp signals when this polyanionic species is included in the running electrolyte. These improvements in analysis are thought to arise as a result of the suppression of coulombic interactions between these positively charged proteins (ion-paired to phytic acid) and the negatively charged silanol groups on the inner wall of the capillary.
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