Separation of tryptophan‐derivative enantiomers with iron‐free human serum transferrin by capillary zone electrophoresis

Ference Kilár, Salvatore Fanali

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

Enantiomers can be separated by using human serum transferrin as a chiral phase. With the help of the native protein we were able to separate enantiomers with high efficiency, using a low ionic strength 2‐(N‐morpholino)ethanesulfonic acid (MES) buffer, pH 6, in capillary zone electrophoresis. Tryptophan methyl, ethyl and butyl ester enantiomers – moving towards the cathode at pH 6 – were resolved by passing through an iron‐free transferrin zone in coated capillaries. Since the isoelectric point of the iron‐free transferrin is a little higher than 6, the protein zone is either not moving in the experiment or is slowly moving towards the anode. Under the simplest experimental conditions the highest resolution was obtained for the butyl ester enantiomers and the lowest for the methyl ester ones. By changing the experimental conditions, however, this order could be reversed. The results indicate that the lengths of the alkyl chains in the enantiomers have a significant effect on the resolution, i.e., on the interaction between the protein and the separands.

Original languageEnglish
Pages (from-to)1510-1518
Number of pages9
JournalELECTROPHORESIS
Volume16
Issue number1
DOIs
Publication statusPublished - 1995

Keywords

  • Capillary zone electrophoresis
  • Chiral separation
  • Enantiomers
  • Human serum transferrin Stereoselective interactions

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry

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