NDLI: Analysis of chemically labile glycation adducts in 2 seed proteins : case study of methylglyoxal-derived 3 hydroimidazolone 1 ( MGH 1 ) 4

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Analysis of chemically labile glycation adducts in 2 seed proteins : case study of methylglyoxal-derived 3 hydroimidazolone 1 ( MGH 1 ) 4

Content Provider	Semantic Scholar
Author	Antonova, Kristina A. Vikhnina, Maria Soboleva, Alena Mehmood, Tahir Heymich, Marie-Louise Leonova, Tatiana Bankin, Mikhail Lukasheva, Elena Gensberger-Reigl, Sabrina Medvedev, Sergei Smolikova, Galina Pischetsrieder, Monika Frolov, Andrej
Copyright Year	2018
Abstract	Seeds represent the major source of food protein, impacting on both human nutrition and 17 animal feeding. Therefore, seed quality needs to be appropriately addressed in the context of 18 viability and food safety. Indeed, long-term and inappropriate storage of seeds might result in 19 enhancement of protein glycation, which might affect their quality and longevity. Glycation of seed 20 proteins can be probed by exhaustive acid hydrolysis and quantification of the glycation adduct 21 Nɛ-(carboxymethyl)lysine (CML) by liquid chromatography-mass spectrometry (LC-MS). This 22 approach, however, does not allow analysis of thermally and chemically labile glycation adducts, 23 like glyoxal-, methylglyoxaland 3-deoxyglucosone-derived hydroimidazolones. Although 24 enzymatic hydrolysis might be a good solution in this context, it requires aqueous conditions, 25 which cannot ensure reconstitution of seed protein isolates. Because of this, the complete profiles of 26 seed AGEs are not characterized so far. Therefore, here we propose the approach, giving access to 27 quantitative solubilization of seed proteins in presence of sodium dodecyl sulfate (SDS) and their 28 quantitative enzymatic hydrolysis prior to removal of SDS by reversed phase solid phase extraction 29 (RP-SPE). Using MG-H1 as a case example, we demonstrate the applicability of this method for 30 reliable and sensitive LC-MS-based quantification of chemically labile AGEs and its compatibility 31 with bioassays. 32
File Format	PDF HTM / HTML
Alternate Webpage(s)	https://www.preprints.org/manuscript/201812.0126/v1/download
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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