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Enrichment of Amadori products derived from the nonenzymatic glycation of proteins using microscale boronate affinity chromatography by Anikó Takátsy; Katalin Böddi; Lívia Nagy; Géza Nagy; Szilvia Szabó; Lajos Markó; István Wittmann; Róbert Ohmacht; Thomas Ringer; Günther K. Bonn; Douglas Gjerde; Zoltán Szabó is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Amadori peptides were enriched using boronate affinity tips and measured by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF/MS). As demonstrated by electrochemical measurements, the tips show the highest binding efficiency for glucose at pH 8.2 employing ammonium chloride/ammonia buffer with ionic strength of 150 mM, exceeding taurine buffer at the same concentration. The bound constituents were released by sorbitol and formic acid. It was also demonstrated that elution with sorbitol at 1.2 M is superior to acidic media. Comparison of results was based on the numbers of detected peptides and their glycated sites. Using sorbitol for elution requires desalting prior to analysis. Therefore, three different sorbents were tested: fullerene-derivatized silica, ZipTip (C18), and C18 silica. Fullerene-derivatized silica and ZipTip showed the same performance regarding the numbers of glycated peptides, and sites were better than C18 silica. The elaborated off-line method was compared with liquid chromatography-tandem mass spectrometry (LC-MS/MS) measurements, by which considerable less modified peptides were detected. Affinity tips used under optimize

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Author

Anikó Takátsy; Katalin Böddi; Lívia Nagy; Géza Nagy; Szilvia Szabó; Lajos Markó; István Wittmann; Róbert Ohmacht; Thomas Ringer; Günther K. Bonn; Douglas Gjerde; Zoltán Szabó

Publisher

Elsevier Science; Elsevier ; Elsevier Inc.; Elsevier BV (ISSN 0003-2697)

Published

2009

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)