Investigation of angiotensin glycosylation by MALDI-TOF and ESI tandem mass spectrometry

Soo Jin Park, Deok Hie Park, Soohwan Sul, Sunghwan F. Oh, In Sook Park, Doo Soo Chung, Hie Joon Kim, Min Sik Kim, Sang-Won Lee

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Angiotensin I, a model decapeptide, was glycosylated and partially hydrolyzed with HCl (6 N, 80 °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.

Original languageEnglish
Pages (from-to)1791-1800
Number of pages10
JournalBulletin of the Korean Chemical Society
Volume25
Issue number12
Publication statusPublished - 2004 Dec 20

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Keywords

  • Angiotensin
  • ESI MS/MS
  • Glycosylation
  • MALDI-TOF MS
  • Partial hydrolysis

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Park, S. J., Park, D. H., Sul, S., Oh, S. F., Park, I. S., Chung, D. S., ... Lee, S-W. (2004). Investigation of angiotensin glycosylation by MALDI-TOF and ESI tandem mass spectrometry. Bulletin of the Korean Chemical Society, 25(12), 1791-1800.