Advanced glycation end products: a highly complex set of biologically relevant compounds detected by mass spectrometry
- 19 April 2001
- journal article
- research article
- Published by Wiley in Journal of Mass Spectrometry
- Vol. 36 (4) , 370-378
- https://doi.org/10.1002/jms.137
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.Keywords
This publication has 28 references indexed in Scilit:
- Alterations in nonenzymatic biochemistry in uremia: Origin and significance of “carbonyl stress” in long-term uremic complicationsKidney International, 1999
- Acid-Stable Fluorescent Advanced Glycation End Products: Vesperlysines A, B, and C Are Formed as Crosslinked Products in the Maillard Reaction between Lysine or Proteins with GlucoseBiochemical and Biophysical Research Communications, 1997
- An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein databaseJournal of the American Society for Mass Spectrometry, 1994
- Immunological quantification of advanced glycosylation end-products in the serum of patients on hemodialysis or CAPDKidney International, 1994
- Reactive glycosylation endproducts in diabetic uraemia and treatment of renal failureThe Lancet, 1994
- A study on in vitro glycation processes by matrix-assisted laser desorption ionization mass spectrometryBiochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, 1993
- Investigation of products arising from enzymatic digestion of advanced glycated albumin by high‐performance liquid chromatography/mass spectrometryRapid Communications in Mass Spectrometry, 1991
- 3-Deoxyglucosone crosslinks proteins under physiological conditions.Agricultural and Biological Chemistry, 1987
- Nonenzymatic Browning in Vivo: Possible Process for Aging of Long-Lived ProteinsScience, 1981
- Lysosomal Enzymes as Agents of Turnover of Soluble Cytoplasmic ProteinsEuropean Journal of Biochemistry, 1975