Investigation of Angiotensin Glycosylation by MALDI-TOF and ESI Tandem Mass Spectrometry

نویسندگان

  • 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
چکیده

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.

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تاریخ انتشار 2004