Advanced glycation end products: a highly complex set of biologically relevant compounds detected by mass spectrometry
✍ Scribed by Annunziata Lapolla; Domenico Fedele; Luigi Martano; Nadia Concetta Arico'; Massimo Garbeglio; Pietro Traldi; Roberta Seraglia; Donata Favretto
- Publisher
- John Wiley and Sons
- Year
- 2001
- Tongue
- English
- Weight
- 239 KB
- Volume
- 36
- Category
- Article
- ISSN
- 1076-5174
- DOI
- 10.1002/jms.137
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✦ Synopsis
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.