Comprehensive analysis of glycated human serum albumin tryptic peptides by off-line liquid chromatography followed by MALDI analysis on a time-of-flight/curved field reflectron tandem mass spectrometer.

@article{Brancia2006ComprehensiveAO,
  title={Comprehensive analysis of glycated human serum albumin tryptic peptides by off-line liquid chromatography followed by MALDI analysis on a time-of-flight/curved field reflectron tandem mass spectrometer.},
  author={Francesco L. Brancia and Jessica Z Bereszczak and Annunziata Lapolla and Domenico Fedele and Lorenzo Baccarin and Roberta Seraglia and Pietro Traldi},
  journal={Journal of mass spectrometry : JMS},
  year={2006},
  volume={41 9},
  pages={1179-85}
}
Glycated peptides arising from in vivo digestion of glycated proteins, usually called advanced glycation end (AGE) product peptides, are biologically relevant compounds due to their reactivity towards circulating and tissue proteins. To investigate their structures, in vitro glycation of human serum albumin (HSA) has been performed and followed by enzymatic digestion. Using different MALDI based approaches the digestion products obtained have been compared with those arising from enzymatic… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 12 extracted citations

Glycated Serum Albumin and AGE Receptors.

Advances in clinical chemistry • 2015

Review: Glycation of human serum albumin.

Clinica chimica acta; international journal of clinical chemistry • 2013
View 1 Excerpt

Similar Papers

Loading similar papers…