Nonenzymatic glycosylation of albumin in vivo. Identification of multiple glycosylated sites.
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Iberg N, Fluckiger R
Nonenzymatic glycosylation of albumin in vivo. Identification of multiple glycosylated sites.
J Biol Chem. 1986 Oct 15;261(29):13542-5.
- PubMed ID
- 3759977 [ View in PubMed]
- Abstract
Nonenzymatic glycosylation of albumin in vivo occurs at multiple sites. Glucose gets attached to Lys-199, Lys-281, Lys-439, and Lys-525 as well as to some other lysine residues. The principal glycosylated site is Lys-525. Approximately 33% of the overall glycosylation occurs at this site. This site specificity is remarkable and is postulated to be a consequence of local catalysis of the nonenzymatic glycosylation reaction. It appears that positively charged amino groups in the protein catalyze the Amadori rearrangement at specific sites. The principal glycosylated site, Lys-525, lies in a Lys-Lys sequence; other glycosylated sites lie in a Lys-Lys, Lys-His, and Lys-His-Lys sequence or are near disulfide bridges, which are likely to place amino groups of more remote parts of the protein closer to these sites. The occurrence of nonenzymatic glycosylation at most of the identified sites in albumin from diabetic patients is explained by the concept of local acid-base catalysis of the Amadori rearrangement.