Sites of Glycation of betaB 2 -Crystallin by Glucose and Fructose

Authors: Zhao H.R.¹; Smith J.B.²; Jiang X.Y.²; Abraham E.C.¹

Source: Biochemical and Biophysical Research Communications, Volume 229, Number 1, December 1996 , pp. 128-133(6)

Buy & download fulltext article:

Price: $52.63 plus tax (Refund Policy)

Abstract:

We determined the sites of glycation of bovine betaB 2 -crystallin by glucose and fructose. After incubation with glucose or fructose, glycated tryptic peptides were purified by affinity chromatography/reverse-phase HPLC and identified by electrospray ionization mass spectrometry (ESIMS). The results gave evidence of glycation at lysine 10, 75, 100, 107, 120, 139, 167 and 171 by both glucose and fructose, while glycated lysine 119 and 47 or 67 were detected only after fructosylation. We conclude that glucose and fructose have similar glycation specificity.

Language: English

Document Type: Research article

Affiliations: 1: Department of Biochemistry and Molecular Biology, Medical College of Georgia, Augusta, Georgia, 30912-2100 2: Department of Chemistry, University of Nebraska, Lincoln, Nebraska, 68588-0304

Publication date: 1996-12-01