Journal article
Electrospray Ionization–Mass Spectrometry Characterization of Heterotetrameric Sarcosine Oxidase
Journal of the American Society for Mass Spectrometry, v 9(5), pp 510-515
1998
PMID: 9879365
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Electrospray ionization (ESI) Fourier transform ion cyclotron resonance (FTICR) mass spectrometry has been used to characterize heterotetrameric corynebacterial sarcosine oxidase. By using a conventional quadrupole mass spectrometer, no spectra for the intact complex could be obtained (i.e., electrospraying protein at neutral pH), but spectra showing the four protein subunits were obtained when electrospraying from acidic solution. Initial low resolution ESI-FTICR mass spectra of the intact heterotetramer revealed a typical narrow charge state distribution in the range 6000 <
m/
z < 9000, consistent with retention of a compact structure in the gas phase, and gave a mass measurement about 1000 u higher than predicted. Efficient in-trap clean up, based upon low energy collisionally induced dissociation of adducts, allowed significant improvement in mass measurement accuracy. The present results represent the largest heteromultimeric protein complex successfully analyzed using FTICR mass spectrometry, and clearly illustrate the importance of sample clean up methods for large molecule characterization.
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Details
- Title
- Electrospray Ionization–Mass Spectrometry Characterization of Heterotetrameric Sarcosine Oxidase
- Creators
- Ljiljana Paša Tolić - Environmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Richland, Washington, USAAmy C Harms - Environmental Molecular Sciences LaboratoryGordon A Anderson - Environmental Molecular Sciences LaboratoryRichard D Smith - Environmental Molecular Sciences LaboratoryAnnie Willie - Allegheny University of the Health SciencesMarilyn Schuman Jorns - Allegheny University of the Health SciencesPacific Northwest National Lab. (PNNL), Richland, WA (United States)
- Publication Details
- Journal of the American Society for Mass Spectrometry, v 9(5), pp 510-515
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- [Retired Faculty]
- Web of Science ID
- WOS:000073226600008
- Scopus ID
- 2-s2.0-0003291379
- Other Identifier
- 991019169005704721
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Data related to this publication, from InCites Benchmarking & Analytics tool:
- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemical Research Methods
- Chemistry, Analytical
- Chemistry, Physical
- Spectroscopy