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Non‐enzymatic glycosylation of the dipeptide l ‐carnosine, a potential anti‐protein‐cross‐linking agent
Author(s) -
Hipkiss Alan R.,
Michaelis Jürgen,
Syrris Petros
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00849-5
Subject(s) - carnosine , chemistry , biochemistry , glycation , dihydroxyacetone , dihydroxyacetone phosphate , glycosylation , dipeptide , enzyme , peptide , glycerol , receptor
The dipeptide carnosine (β‐alanyl‐ l ‐histidine) was readily glycosylated non‐enzymatically upon incubation with the sugars glucose, galactose, deoxyribose and the triose dihydroxyacetone. Carnosine inhibited glycation of actyl‐Lys‐His‐amide by dihydroxyacetone and it protected α‐crystallin, superoxide dismutase and catalise against glycation and cross‐linking mediated by ribose, deoxyribose, dihydroxyacetone, dihydroxyacetone phosphate and fructose. Unlike certain glycated amino acids, glycated carnosine was non‐mutagenic. The potential biological and therapeutic significance of these observations are discussed.