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
  • *Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    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
    DOIs
    Publication statusPublished - 2004 Dec 20

    Keywords

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

    ASJC Scopus subject areas

    • General Chemistry

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