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Characterization and sequence identification of angiotensin II by a novel method involving ultra-fast liquid chromatography assay coupled with matrix-assisted laser desorption/ionization quadrupole ion trap time-of-flight five tandem mass spectrometry analysis
KTH, School of Biotechnology (BIO).
2010 (English)In: European journal of mass spectrometry, ISSN 1469-0667, E-ISSN 1751-6838, Vol. 16, no 6, 663-671 p.Article in journal (Refereed) Published
Abstract [en]

High-throughput proteomics aims to investigate dynamically changing proteins expressed by a full organism, specific tissue or cellular compartment under certain conditions. High-sensitivity mass spectrometry has gradually become a significant tool for characterizing peptides. Here, we analyzed angiotensin II using ultra-fast liquid chromatography (UFLC) coupled with matrix-assisted laser desoprtion/ionization time-of-flight mass spectrometry (MALDI-ToF MS5). First, we applied UFLC in isolating and collecting the angiotensin II, and then Axima-Resonance (MALDI-QIT-ToF MS5) was adopted, which enables collision-induced dissociation-MS5 analysis for fine structural characterization of angiotensin II. Resultant MS, MS2, MS3 and MS4 spectra of interested [M+H](+) ions selected as precursor ions yielded detailed information about the sites of fragmentation as well as the amino acid sequence for angiotensin II; meanwhile, the average deviation between theoretical mass and actually measured mass from MS to MS5 spectra was only 0.32 Da. It indicated that Axima-Resonance was capable of analysing the peptide sequence accurately and providing the corresponding fragmentation information thoroughly, thus suggesting a potential strategy involving UFLC assay coupled with MALDI-QIT-ToF MS5 analysis for high-throughput proteomics studies in the future.

Place, publisher, year, edition, pages
2010. Vol. 16, no 6, 663-671 p.
Keyword [en]
angiotensin II, UFLC, MALDI-QIT-ToF MS5, Axima-Resonance
National Category
Industrial Biotechnology
Identifiers
URN: urn:nbn:se:kth:diva-31355DOI: 10.1255/ejms.1099ISI: 000287620300004Scopus ID: 2-s2.0-78650834334OAI: oai:DiVA.org:kth-31355DiVA: diva2:404404
Note
QC 20110317Available from: 2011-03-17 Created: 2011-03-14 Last updated: 2017-12-11Bibliographically approved

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CiteExportLink to record
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