Comparative analysis of somatostatin analog peptides by capillary electrophoresis and micellar elektrokinetic chromatography

Miklós Idei, Imre Mezö, Zsolt Vadász, Anikó Horváth, János Seprödi, Judit Érchegyi, István Teplán, György Kéri

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6 Citations (Scopus)


Capillary electrophoresis (CE) and micellar electrokinetic chromatography (MEKC) methods, utilizing uncoated silica capillary and triethyl ammonium phosphate or sodium borate buffers in the pH range of 2.25-11.0, containing sodium dodecyl sulfate (SDS) (0-100 mM) for analysis of somatostatin-analog peptides were developed. The method presented here was compared with the reversed-phase high performance liquid chromatographic (RP-HPLC) and CE methods developed for analysis of peptides. The peptides investigated in this work can be separated by CE on the basis of their electrophoretic mobility in aqueous buffer of low pH value (pH 2.25) or by MEKC on the basis of their hydrophobicity in SDS containing buffer of high pH value (pH 11.0). Optimal MEKC separation of the investigated peptides has been achieved at pH 11.0 in an Na-borate buffer containing 100 mM SDS. CE at pH 2.25 proved insensitive to the hydrophobicity of the peptides investigated. By contrast, results obtained with MEKC at pH 11.0 proved to be anologous to those obtained by RP-HPLC, with highly hydrophobic peptides - migrating slower than peptides without hydrophobic moieties.

Original languageEnglish
Pages (from-to)758-761
Number of pages4
Issue number4
Publication statusPublished - Apr 1996



  • Capillary electrophoresis
  • Micellar electrokinetic chromatography
  • Somatostatin analog peptides

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Clinical Biochemistry

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