Bulletin of the Korean Chemical Society

Korean Chemical Society (대한화학회)
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Investigation of Angiotensin Glycosylation by MALDI-TOF and ESI Tandem Mass Spectrometry

  • Park, Soo-Jin (School of Chemistry, Seoul National University) ;
  • Park, Deok-Hie (LG Chem, Ltd.) ;
  • Sul, Soo-Hwan (Department of Chemistry, University of California) ;
  • Oh, Sung-Hwan F. (Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School) ;
  • Park, In-Sook (School of Chemistry, Seoul National University) ;
  • Chung, Doo-Soo (School of Chemistry, Seoul National University) ;
  • Kim, Hie-Joon (School of Chemistry, Seoul National University) ;
  • Kim, Min-Sik (Department of Chemistry and Center for Electro- & Photo-Responsive Molecules, Korea University) ;
  • Lee, Sang-Won (Department of Chemistry and Center for Electro- & Photo-Responsive Molecules, Korea University)
  • Published : 2004.12.20
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Abstract

Angiotensin I, a model decapeptide, was glycosylated and partially hydrolyzed with HCl (6 N, 80 $^{\circ}C$, 4 h), aminopeptidase, and carboxypeptidase Y. A single peptide mass map obtained from truncated peptides in the partial acid hydrolysate of angiotensin and its glycosylation product mixture by matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry enabled sequencing of angiotensin by a combinatorial procedure. MALDI-TOF and electrospray ionization (ESI) tandem mass spectrometric results indicate that both the N-terminal amino group of aspartic acid and the guanidinium group of the second residue arginine are glycosylated.

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References

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