Candidate reference methods for hemoglobin A1c based on peptide mapping

Clin Chem. 1997 Oct;43(10):1944-51.

Abstract

A reference method that specifically measures hemoglobin (Hb) A1c is an essential part of the reference system for the international standardization of Hb A1c/glycohemoglobin. We have developed a new method for quantification, based on the specific N-terminal residue of the hemoglobin beta-chains. Enzymatic cleavage of the intact hemoglobin molecule with endoproteinase Glu-C has been optimized to obtain the beta-N-terminal hexapeptides of Hb A1c and Hb A0. These peptides have been separated by reversed-phase HPLC and quantitated by electrospray ionization-mass spectrometry (method A) or by capillary electrophoresis (method B). With these peptides and hyphenated separation techniques, it has been possible to overcome the insufficient resolution of currently used protein separation systems for Hb A1c.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chromatography, High Pressure Liquid / methods
  • Electrophoresis, Capillary / methods
  • Glycated Hemoglobin / analysis*
  • Humans
  • Mass Spectrometry / methods
  • Peptide Mapping
  • Reference Values

Substances

  • Glycated Hemoglobin A