21
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      Advanced glycation end products: a highly complex set of biologically relevant compounds detected by mass spectrometry.

      Journal of Mass Spectrometry
      Animals, Cattle, Chromatography, High Pressure Liquid, Glycosylation End Products, Advanced, analysis, In Vitro Techniques, Reproducibility of Results, Serum Albumin, Bovine, chemistry, Spectrometry, Fluorescence, methods, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Spectrometry, Mass, Secondary Ion, Spectrophotometry, Ultraviolet

      Read this article at

      ScienceOpenPublisherPubMed
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Structural information on 'AGE-peptides,' a class of substances belonging to advanced glycation end products (AGE) and originating by proteolysis of glycated proteins, was gained through various analytical approaches on the mixture produced by proteinase K digestion of in vitro glycated bovine serum albumin. Both matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) and high-performance liquid chromatography/electrospray ionization mass spectrometry (HPLC/ESI-MS) were employed, and the results were compared with those from conventional spectroscopic methods (UV, fluorescence, gel permeation). The data acquired by the various techniques all depict the digestion mixtures as highly complex, with components exhibiting molecular mass in the range 300-3500 Da. In the analysis of HPLC/ESI-MS data, identification of AGE-peptides was facilitated by 3D mapping. Structural information was gained by means of multiple mass spectrometric experiments. Copyright 2001 John Wiley & Sons, Ltd.

          Related collections

          Author and article information

          Comments

          Comment on this article