Skip to content Skip to navigation
University of Warwick
  • Study
  • |
  • Research
  • |
  • Business
  • |
  • Alumni
  • |
  • News
  • |
  • About

University of Warwick
Publications service & WRAP

Highlight your research

  • WRAP
    • Home
    • Search WRAP
    • Browse by Warwick Author
    • Browse WRAP by Year
    • Browse WRAP by Subject
    • Browse WRAP by Department
    • Browse WRAP by Funder
    • Browse Theses by Department
  • Publications Service
    • Home
    • Search Publications Service
    • Browse by Warwick Author
    • Browse Publications service by Year
    • Browse Publications service by Subject
    • Browse Publications service by Department
    • Browse Publications service by Funder
  • Help & Advice
University of Warwick

The Library

  • Login
  • Admin

Ion mobility augments the utility of mass spectrometry in the identification of human hemoglobin variants

Tools
- Tools
+ Tools

Williams, Jonathan P., Giles, K. (Kevin), Green, Brian N., Scrivens, James H. and Bateman, R. H. (Robert H.) (2008) Ion mobility augments the utility of mass spectrometry in the identification of human hemoglobin variants. Rapid Communications in Mass Spectrometry, Vol.22 (No.20). pp. 3179-3186. doi:10.1002/rcm.3718

Research output not available from this repository, contact author.
Official URL: http://dx.doi.org/10.1002/rcm.3718

Request Changes to record.

Abstract

The global dispersion of hemoglobin variants through population migration has precipitated a need for their identification. A particularly effective mass spectrometry (MS)-based procedure involves analysis of the intact globin chains in diluted blood to detect the variant through mass anomalies, followed by location of the variant amino acid residue by direct analysis of the enzymatically digested globins. Here we demonstrate the use of ion mobility separation in combination with this MS procedure to reduce mass spectral complexity. In one example, the doubly charged tryptic peptide from a low abundance variant (4%) occurred at the same m/z value as a singly and a doubly charged interfering ion. In another example, the singly charged tryptic peptide from an alpha-chain variant (26%) occurred at the same m/z value as a doubly charged interfering ion. Ion mobility was used to separate the variant ions from the interfering ions, thus allowing the variant peptides to be observed and sequenced by tandem mass spectrometry. Copyright (C) 2008 John Wiley & Sons, Ltd.

Item Type: Journal Article
Subjects: Q Science > QD Chemistry
Q Science > QP Physiology
Divisions: Faculty of Science > Life Sciences (2010- ) > Biological Sciences ( -2010)
Faculty of Science > Chemistry
Library of Congress Subject Headings (LCSH): Ion mobility spectroscopy, Mass spectrometry, Hemoglobin polymorphisms
Journal or Publication Title: Rapid Communications in Mass Spectrometry
Publisher: John Wiley & Sons Ltd.
ISSN: 0951-4198
Official Date: October 2008
Dates:
DateEvent
October 2008Published
Volume: Vol.22
Number: No.20
Number of Pages: 8
Page Range: pp. 3179-3186
DOI: 10.1002/rcm.3718
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access
Funder: Wellcome Trust (London, England)

Data sourced from Thomson Reuters' Web of Knowledge

Request changes or add full text files to a record

Repository staff actions (login required)

View Item View Item
twitter

Email us: wrap@warwick.ac.uk
Contact Details
About Us