Model studies on protein glycation: influence of cysteine on the reactivity of arginine and lysine residues toward glyoxal.
Ann N Y Acad Sci
; 1126: 248-52, 2008 Apr.
Article
en En
| MEDLINE
| ID: mdl-18448824
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.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Arginina
/
Glicosilación
/
Cisteína
/
Glioxal
/
Lisina
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
Ann N Y Acad Sci
Año:
2008
Tipo del documento:
Article
País de afiliación:
Alemania