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. ISSN 0951-4198

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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
Volume:	Vol.22
Number:	No.20
Number of Pages:	8
Page Range:	pp. 3179-3186
Identification Number:	10.1002/rcm.3718
Status:	Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Restricted or Subscription Access
Funder:	Wellcome Trust (London, England)
References:	1. Hardison RC, Chui DHK, Giardine B, Riemer C, Patrinos GP, Anagnou N, Miller W, Wajcman H. Hum. Mutat. 2002; 19: 225. Available: http://globin.cse.psu.edu. 2. Wild BJ, Green BN, Cooper EK, Lalloz MRA, Erten S, Stephens AD, Layton DM. Blood Cells Mol. Dis. 2001; 27: 691. 3. Rai DK, Griffiths WJ, Landin B, Wild BJ, Alvelius G, Green BN. Anal. Chem. 2003; 75: 1978. 4. Giles K, Pringle SD, Worthington KR, Little D, Wildgoose JL, Bateman RH. Rapid Commun. Mass Spectrom. 2004; 18: 2401. 5. Pringle SD, Giles K, Wildgoose JL, Williams JP, Slade SE, Thalassinos K, Bateman RH, Bowers MT, Scrivens JH. Int. J. Mass Spectrom. 2007; 261: 1. 6. Schneider RG, Brimhall B, Jones RT, Bryant R, Mitchell CB, Goldberg AI. Biochim. Biophys. Acta 1971; 243: 164. 7. Rosa J, Maleknia N, Vergoz D, Dunet R. Nouv. Rev. Fr. D’Hematol. 1965; 6: 423. 8. Valentine SJ, Counterman AE, Hoaglund CS, Reilly JP, Clemmer DE. J. Am. Soc. Mass Spectrom. 1998; 9: 1213. 9. Valentine SJ, Counterman AE, Clemmer DE. J. Am. Soc. Mass Spectrom. 1999; 10: 1188. 10. Williams JP, Scrivens JH, Giles K, Green BN, Bateman RH. Proc. 55th ASMS Conf. Mass Spectrometry and Allied Topics, Indianapolis, Indiana, USA, 2007; TP 057.
URI:	http://wrap.warwick.ac.uk/id/eprint/29113

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