Literature DB >> 8954094

Sites of glycation of beta B2-crystallin by glucose and fructose.

H R Zhao1, J B Smith, X Y Jiang, E C Abraham.   

Abstract

We determined the sites of glycation of bovine beta B2-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.

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Year:  1996        PMID: 8954094     DOI: 10.1006/bbrc.1996.1768

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  2 in total

Review 1.  Formation of Fructose-Mediated Advanced Glycation End Products and Their Roles in Metabolic and Inflammatory Diseases.

Authors:  Alejandro Gugliucci
Journal:  Adv Nutr       Date:  2017-01-17       Impact factor: 8.701

2.  Gamma III-crystallin is the primary target of glycation in the bovine lens incubated under physiological conditions.

Authors:  Hong Yan; Antony C Willis; John J Harding
Journal:  Biochem J       Date:  2003-09-15       Impact factor: 3.857

  2 in total

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