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Identification of the site of glycation of human insulin

Biomedical Sciences Research Institute Computer Science Research Institute Environmental Sciences Research Institute Nanotechnology & Advanced Materials Research Institute

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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Abstract

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:11 Jun 2010 13:22

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