Carnosine promotes the heat denaturation of glycated protein
Laboratory studyOther animals
- Design
- Laboratory study
- What was measured
- Thermal denaturation parameters (T0.5, Gibbs free energy barrier and enthalpy) of cytosolic aspartate aminotransferase glycated with 500 microM glyceraldehyde, with and without carnosine.
What the authors reported
Glycation raised the denaturation temperature, free energy barrier and enthalpy of the enzyme. Carnosine enhanced thermal unfolding of the glycated protein, lowering T0.5, the free energy barrier and the enthalpy of denaturation, which the authors interpret as carnosine promoting hydration and tagging glycated proteins for removal.
Limits of this study
Model protein in vitro. Abstract only.
Source
PubMed 12480523 · doi:10.1016/s0006-291x(02)02796-1
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.