Document Detail

Identification of glycation at the N-terminus of albumin by gas chromatography-mass spectrometry.
MedLine Citation:
PMID:  2803249     Owner:  NLM     Status:  MEDLINE    
Amino groups in human albumin are modified in vivo by glucose in a non-enzymic reaction, and previous studies have implicated lysine residues as exclusive participants. An investigation using g.c.-m.s. was undertaken to ascertain whether or not the N-terminus was also involved. Appropriate model compounds [N-(1-deoxyglucitol-1-yl) and N-(1-deoxymannitol-1-yl) adducts of aspartic acid] were synthesized and the diagnostic fragment ions of suitable derivatives were established under electron-impact and negative-chemical-ionization conditions. Characteristic fragment ions were identical with those obtained from the model compounds in the mass spectra of derivatives prepared from hydrolysates of reduced albumin. A purified mixture of the model compounds was also obtained from such hydrolysates. Use of radioisotopic incorporation demonstrated that the relative extent of glycation of the epsilon-amino and alpha-amino groups in albumin was approx. 8:1. N-1-Deoxyhexitol adducts of aspartic acid were also identified in reduced and hydrolysed peptides of human urine.
D A Robb; O S Olufemi; D A Williams; J M Midgley
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Biochemical journal     Volume:  261     ISSN:  0264-6021     ISO Abbreviation:  Biochem. J.     Publication Date:  1989 Aug 
Date Detail:
Created Date:  1989-11-09     Completed Date:  1989-11-09     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  871-8     Citation Subset:  IM    
Department of Bioscience and Biotechnology, University of Strathclyde, Glasgow, Scotland, U.K.
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MeSH Terms
Gas Chromatography-Mass Spectrometry
Reg. No./Substance:
0/Albumins; 50-99-7/Glucose

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