A ginseng polypeptide (GPP) found in ginseng roots and its modified pe
ptides were tested by capillary zone electrophoresis (CZE) under acidi
c as well as basic conditions. Modified peptides were synthesized for
three purposes: (i) to analyze their functions in the first three acid
ic amino acid residues, (ii) to analyze their functions in three seque
nced glycines, and (iii) to analyze the length of side chains in acidi
c amino acids. The roles of glycines, acidic amino acids and amino aci
d side chains in the binding of Mg2+ were studied at pH values less th
an 7.0. The migration times of GPP varied with the pH of various elect
rophoresis buffers, and electrophoresis patterns were significantly ch
anged between pH 7.0-7.5. Based on the electrophoretic analysis, it wa
s concluded that the binding mechanisms for Mg2+ or conformations of G
PP changed between low pH and high pH.