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. 1989 Aug 1;261(3):871–878. doi: 10.1042/bj2610871

Identification of glycation at the N-terminus of albumin by gas chromatography-mass spectrometry.

D A Robb 1, O S Olufemi 1, D A Williams 1, J M Midgley 1
PMCID: PMC1138911  PMID: 2803249

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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