Separation of closely related large peptides by micellar electrokinetic chromatography with organic modifiers.
Large peptides with similar electrophoretic mobilities were separated by micellar electrokinetic chromatography (MEKC) with organic modifiers. [Leu13]motilin and [Met13]motilin differ by only one neutral amino acid residue. Because the electrophoretic mobilities of these peptides are almost identical, these peptides were not separated by capillary zone electrophoresis (CZE). Such large peptides have not been separated by conventional MEKC either, because they interacted strongly with the micelle. However, they were completely separated by MEKC when an organic solvent was added to the micellar solution. Some insulins, larger peptides than motilin, from different origins, which have very similar electrophoretic mobilities, were also successfully separated by the same technique. The size of peptides which were separated without organic modifiers was examined.
Yashima
T
T
Pharmaceutical Research Laboratories, Kyowa Hakko Kogyo Company, Ltd., Shizuoka, Japan.
Tsuchiya
A
A
Morita
O
O
Terabe
S
S
D000595:Amino Acid Sequence; D000818:Animals; D002853:Chromatography, Liquid / Q000379:methods*; D006863:Hydrogen-Ion Concentration; D007328:Insulin / Q000737:chemistry / Q000302:isolation & purification; D008823:Micelles; D008969:Molecular Sequence Data; D009037:Motilin / Q000031:analogs & derivatives / Q000737:chemistry / Q000302:isolation & purification; D010455:Peptides / Q000737:chemistry / Q000302:isolation & purification*; D013552:Swine
D007328:Insulin; D008823:Micelles; D010455:Peptides; D009037:Motilin