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http://dx.doi.org/10.5012/bkcs.2004.25.12.1791

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)
Publication Information
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.
Keywords
Angiotensin; Glycosylation; Partial hydrolysis; MALDI-TOF MS; ESI MS/MS;
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