Analysis of glycated amino acids by high-performance liquid chromatography of phenylthiocarbamyl derivatives

Donald J. Walton, John Douglas Mcpherson

Research output: Contribution to journalArticle

15 Scopus citations

Abstract

A method has been developed for the analysis of hexitolamino acids formed by acid-catalyzed hydrolysis of nonenzymatically glycated proteins that have been treated with sodium borohydride. The hexitolamino acids are converted into phenylthiocarbamyl (PTC) derivatives which are analyzed by reverse-phase HPLC. The PTC derivatives of Nα-hexitolamino acids behave like lactones, migrating on the column more slowly than the corresponding PTC-amino acids. The PTC derivatives of Nε{lunate}-glucitol- and Nε{lunate}-mannitol-lysine are probably free acids, since they migrate faster than PTC-lysine. The method, which can be used to determine the degree of glycation of N-terminal and lysyl residues, has been applied successfully to human hemoglobin, serum albumin, and ocular lens proteins.

Original languageEnglish (US)
Pages (from-to)547-553
Number of pages7
JournalAnalytical Biochemistry
Volume164
Issue number2
DOIs
StatePublished - Aug 1 1987
Externally publishedYes

Keywords

  • glycation of proteins
  • HPLC of amino acid derivatives
  • nonenzymatic glycosylation

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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