Mass Spectrometry Characterization of the Glycation Sites of Bovine Insulin by Tandem Mass Spectrometry

21Citations
Citations of this article
33Readers
Mendeley users who have this article in their library.

Abstract

Bovine insulin was glycated under hyperglycemic reducing conditions and in nonreducing conditions. Purification through HPLC allowed isolating glycated forms of insulin and a novel triglycated form (6224.5 Da) was purified. Endoproteinase Glu-C digestion combined with mass spectrometry (MALDI-TOF/TOF) allowed determining the exact location of the glycation sites in each of the isolated glycated insulins. For the first time, a triglycated form of insulin was isolated and characterized accordingly to its glycation sites. These glucose binding sites were identified as the N-terminals of both chains (Gly1 and Phe1) and residue Lys29 of B-chain. Moreover, in diglycated insulin we found the coexistence of one specie glycated at the N-terminals of both chains (Gly1 and Phe1) and another specie containing the two glucitol adducts in B-chain (Phe1 and Lys29). Also, in monoglycated insulin generated in reducing and nonreducing conditions, one specie glycated at Phe1 and another specie glycated at Lys29, both B-chain residues coexist. © 2009 American Society for Mass Spectrometry.

Cite

CITATION STYLE

APA

Guedes, S., Vitorino, R., Domingues, M. R. M., Amado, F., & Domingues, P. (2009). Mass Spectrometry Characterization of the Glycation Sites of Bovine Insulin by Tandem Mass Spectrometry. Journal of the American Society for Mass Spectrometry, 20(7), 1319–1326. https://doi.org/10.1016/j.jasms.2009.03.004

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free