Site specificity of glycation and carboxymethylation of bovine serum albumin by fructose

D.J.S. Hinton, Jennifer Ames

Research output: Contribution to journalArticle

50 Citations (Scopus)

Abstract

We report an investigation of the site specificity, extent and nature of modification of bovine serum albumin (BSA) incubated with fructose or glucose at physiological temperature and pH. Sites of early glycation (Heyns rearrangement products (HRP) from fructose; fructoselysine (FL) from glucose) as well as advanced glycation (N-epsilon-(carboxymethyl)lysine; CML) wereanalyzed by liquid chromatography-mass spectrometry. The major site of modification by fructose, like glucose, is Lysine-524 and this results in, respectively, 31 and 76% loss of the corresponding unmodified tryptic peptide, Gln525-Lys533. In addition, total lysine, HRP, FL, CML and N-epsilon-(carboxyethyl)lysine in the incubations, was quantified. Almost all of the loss of lysine in the fructose-modified BSA was attributed to the formation of CML, with the yield of CML being up to 17-fold higher than glucose-modified BSA. A mechanism for the formation of CML from the HRP is proposed.
Original languageEnglish
Pages (from-to)425-433
Number of pages9
JournalAmino Acids
Volume30(4)
Issue number4
DOIs
Publication statusPublished - Jun 2006

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Biochemistry
  • Endocrinology

Fingerprint Dive into the research topics of 'Site specificity of glycation and carboxymethylation of bovine serum albumin by fructose'. Together they form a unique fingerprint.

  • Cite this