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Chromatographia

, Volume 34, Issue 9–10, pp 493–496 | Cite as

Separation of closely related peptides by capillary electrophoresis with a nonionic surfactant

  • N. Matsubara
  • S. Terabe
Originals

Summary

Separation of Angiotensin II, its derivatives and motilins, which have the same electric charge but a single different amino acid, was performed by capillary electrophoresis with a micellar pseudo-phase of nonionic surfactant, Tween 20, in the solution. The weak interaction of the micelles with the peptides enabled the separation of motilins, peptides with a long chain length. Under these conditions, the micellar phase worked more like a stationary phase in liquid chromatography.

Key Words

Capillary electrophoresis Nonionic micelles Tween 20 Angiotensin II Motilin 

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Copyright information

© Friedr. Vieweg & Sohn Verlagsgesellschaft mbH 1992

Authors and Affiliations

  • N. Matsubara
    • 1
  • S. Terabe
    • 1
  1. 1.Faculty of ScienceHimeji Institute of TechnologyHyogoJapan

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