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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 25, Number 12
BKCSDE 25(12)
December 20, 2004 

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
Angiotensin, Glycosylation, Partial hydrolysis, MALDI-TOF MS, ESI MS/MS
Angiotensin I, a model decapeptide, was glycosylated and partially hydrolyzed with HCl (6 N, 80 oC, 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.
1791 - 1800
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