Carnosine reacts with a glycated protein
Laboratory studyOther animals
- Design
- Laboratory study
- What was measured
- Carbonyl groups on ovalbumin treated with methylglyoxal, incorporation of 14C-carnosine into the glycated protein, and cross-linking of the glycated protein to lysine and to alpha-crystallin.
What the authors reported
Incubation of methylglyoxal-treated ovalbumin with carnosine accelerated the decline in protein carbonyl groups. Radiolabelled carnosine became bound to the glycated protein (a TCA-precipitable product), which was not seen with untreated protein, and lysine or an acetylglycyl-lysine ester reduced this binding. Carnosine also inhibited cross-linking of the glycated ovalbumin to lysine and to alpha-crystallin. The authors term the reaction carnosinylation and propose it as a route for inactivating or removing carbonyl-bearing proteins.
Limits of this study
Test-tube chemistry with a model protein; whether the reaction occurs inside cells was not tested. Abstract only.
Source
PubMed 10927182 · doi:10.1016/s0891-5849(00)00270-7
Entry checked against PubMed abstract (E-utilities) on 2026-10-19. The dose shown is the dose the researchers used. It is not a recommendation. How to read this page.