Spectroscopic studies of the protein-methylglyoxal adduct.

AUTOR(ES)

McLaughlin, J A

RESUMO

Spectroscopic measurements are reported for the effects of pH, time, solvent, and chemical modification of arginine and lysine side chains on the reaction of proteins with methylglyoxal. The reaction responsible for the appearance of a brown coloration and increased submolecular electronic activity in the proteins involves the epsilon-amino groups of the lysine residues. It is concluded that the primary step in the reaction involves the formation of a Schiff base linkage between the lysine side chain and methylglyoxal. These findings reaffirm the concept that, by the formation of Schiff bases, aldehydes can act as electron acceptors in charge transfer interactions with proteins.

Documentos Relacionados

• Electronic properties of some protein--methylglyoxal complexes.
• Mutational properties of the primary aflatoxin B1-DNA adduct.
• Human and E.coli excinucleases are affected differently by the sequence context of acetylaminofluorene-guanine adduct.
• Reaction of DNA with chemically or enzymatically activated mitomycin C: isolation and structure of the major covalent adduct.
• Facile formation of a crosslinked adduct between DNA and the daunorubicin derivative MAR70 mediated by formaldehyde: molecular structure of the MAR70-d(CGTnACG) covalent adduct.