Anti-crosslinking properties of carnosine: significance of histidine
Laboratory studyOther animals
- Design
- Laboratory study
- Subjects
- not applicable (enzyme glycation assays)
- Dose used in the study
- not stated in abstract
- Duration
- not stated in abstract
- What was measured
- Glycation-induced crosslinking of cytosolic aspartate aminotransferase in the presence of carnosine, beta-alanine, histidine, alpha-acetyl-histidine, 1-methyl-histidine and anserine.
What the authors reported
The authors report that beta-alanine had weaker anti-crosslinking activity than carnosine, that histidine was more effective than carnosine itself, and that acetylating the alpha-amino group or methylating the imidazole of histidine removed its activity. Methylating carnosine's imidazole (anserine) reduced activity. They conclude that histidine is the representative structure for an anti-crosslinking agent and propose that the imidazolium group stabilises adducts formed at the primary amino group.
Limits of this study
Cell-free protein glycation model; no cell, animal or human data.
Source
PubMed 15234195 · doi:10.1016/j.lfs.2004.05.002
Entry checked against abstract (Kansas City University Digital Commons record) on 2026-10-11. The dose shown is the dose the researchers used. It is not a recommendation. How to read this page.