Separation optimization of the molecular forms of transferrin complexes by capillary zone electrohoresis

Judit Gálicza, Viktor Sándor, Andrea Vargová, Beáta Ábrahám, Szabolcs Lányi, Ferenc Kilár

Research output: Contribution to journalArticle

Abstract

Human serum transferrin (Tf), a glycoprotein, has two lobes, each having a binding site for trivalent iron ions. The binding of metal ions and different anions (oxalate, aziridine-carboxylate, bicarbonate) to these binding site results four different molecular form of Tf (holo-Tf, diferri FeNTfFeC, and monoferri TfFeN, TfFeC). High performance capillary zone electrophoresis (CZE) experiments were performed in order to separate these molecular forms. We changed the following separation conditions: background electrolyte, capillary treatment and voltage to achieve high efficiency of separation of transferrin probes after the complexation reaction.

Original languageEnglish
Pages (from-to)153-164
Number of pages12
JournalUPB Scientific Bulletin, Series B: Chemistry and Materials Science
Volume74
Issue number2
Publication statusPublished - Aug 23 2012

Keywords

  • Capillary zone electrophoresis
  • Transferrin

ASJC Scopus subject areas

  • Chemistry(all)
  • Materials Science(all)

Fingerprint Dive into the research topics of 'Separation optimization of the molecular forms of transferrin complexes by capillary zone electrohoresis'. Together they form a unique fingerprint.

  • Cite this