Model studies on protein glycation - Influence of cysteine on the reactivity of arginine and lysine residues toward glyoxal
Research output: Contribution to book/Conference proceedings/Anthology/Report › Conference contribution › Contributed › peer-review
Contributors
Abstract
Mixtures of N-alpha-hippurylarginin, N-alpha-hippuryllysine, and glyoxal were incubated in the absence and presence of N-alpha-acetylcysteine in order to assess the individual reactivity of these nucleophilic amino acid residues. The incubations were performed under atmospheric and high hydrostatic pressure (400 MPa), and, at the same time, beta-casein was reacted with glyoxal. The results showed that arginine is the main partner for glyoxal in the absence of cysteine, whereas a lysine derivatization was not apparent. In the presence of cysteine, however, arginine was almost completely protected from the reaction, whereas a noticeable formation of lysine derivatives, mainly carboxymethyllysine, was observed. Based on these findings, a reaction mechanism is proposed to explain the influence of cysteine on the reaction.
Details
Original language | English |
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Title of host publication | MAILLARD REACTION: RECENT ADVANCES IN FOOD AND BIOMEDICAL SCIENCES |
Editors | E Schleicher, Somoza, P Shieberle |
Publisher | Blackwell Publishing |
Pages | 248-252 |
Number of pages | 5 |
ISBN (print) | 978-1-57331-719-1 |
Publication status | Published - 2008 |
Peer-reviewed | Yes |
Publication series
Series | Annals of the New York Academy of Sciences |
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Volume | 1126 |
ISSN | 0077-8923 |
Conference
Title | 9th International Symposium on the Maillard Reaction |
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Duration | 1 September 2007 |
City | Munich |
Country | Germany |
External IDs
Scopus | 42549164542 |
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Keywords
Keywords
- carboxymethyllysine, glyoxal, nucleophilic amino acids, high hydrostatic pressure, MAILLARD REACTION