HIPKISS, AR; MICHAELIS, J; SYRRIS, P; (1995) NONENZYMATIC GLYCOSYLATION OF THE DIPEPTIDE L-CARNOSINE, A POTENTIAL ANTI-PROTEIN-CROSS-LINKING AGENT. FEBS LETT , 371 (1) 81 - 85.
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The dipeptide carnosine (beta-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 alpha-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 cion-mutagenic. The potential biological and therapeutic significance of these observations are discussed.
|Title:||NONENZYMATIC GLYCOSYLATION OF THE DIPEPTIDE L-CARNOSINE, A POTENTIAL ANTI-PROTEIN-CROSS-LINKING AGENT|
|Keywords:||CARNOSINE, NONENZYMATIC GLYCOSYLATION, DIABETES, AGING, AGE-PRODUCT, DIABETES-MELLITUS, MAILLARD REACTION, GLYCATION, GLUCOSE, IDENTIFICATION, MUTAGENICITY, POLYPEPTIDES, PROTECTION|
|UCL classification:||UCL > School of Life and Medical Sciences > Faculty of Population Health Sciences > Institute of Cardiovascular Science|
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