Carnosine disaggregates glycated alpha-crystallin: an in vitro study
Laboratory studyOther animals
- Design
- Laboratory study
- What was measured
- Light scattering at 90 degrees and tryptophan fluorescence polarisation of methylglyoxal-glycated alpha-crystallin after addition of carnosine, guanidine-HCl or urea.
What the authors reported
Methylglyoxal glycation aggregated alpha-crystallin, raising light scattering; after carnosine was added, scattering returned to baseline, indicating smaller aggregates. Carnosine also lowered tryptophan fluorescence polarisation, suggesting increased peptide chain mobility. Guanidine and urea had no effect.
Limits of this study
In vitro lens protein model; the abstract's reference to carnosine reversing lens opacity in human trials is background, not a result of this study. Abstract only.
Source
PubMed 15178493 · doi:10.1016/j.abb.2004.04.024
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.