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Identification of the site of glycation of human insulin

O'Harte, Finbarr, Hojrup, P, Barnett, CR and Flatt, Peter (1996) Identification of the site of glycation of human insulin. PEPTIDES, 17 (8). pp. 1323-1330. [Journal article]

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This study evaluates the nature of glycated human insulin formed following exposure to hyperglycemic conditions in vitro. Glycated insulin was purified by RP-HPLC and its molecular mass (5971.3 Da) determined by plasma desorption mass spectrometry (MS). The difference in mass (163.7 Da) from nonglycated insulin (5807.6 Da) corresponds to a single reduced glucose (glucitol) residue. Following reduction of insulin disulfide bridges, MS confirmed that the B-chain was glycated. Enzymatic digestions with trypsin, endoproteinase Glu-C, and thermolysin, followed by RP-HPLC and identification of fragments by MS, localized glycation to the B-chain (1-5) region. Electrospray tandem MS identified the site of glycation as the B-chain NH2-terminal Phe(1) residue. This was confirmed by automated Edman degradation with glycated human insulin. Copyright (C) 1996 Elsevier Science Inc.

Item Type:Journal article
Faculties and Schools:Faculty of Life and Health Sciences
Faculty of Life and Health Sciences > School of Biomedical Sciences
Research Institutes and Groups:Biomedical Sciences Research Institute
Biomedical Sciences Research Institute > Diabetes
ID Code:3148
Deposited By: Professor Peter Flatt
Deposited On:08 Jan 2010 13:14
Last Modified:09 May 2016 10:48

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