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]
Full text not available from this repository.
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
|Deposited By:||Professor Peter Flatt|
|Deposited On:||08 Jan 2010 13:14|
|Last Modified:||09 May 2016 10:48|
Repository Staff Only: item control page