Hot Electron Capture Dissociation Distinguishes Leucine from Isoleucine in a Novel Hemoglobin Variant, Hb Askew, beta 54(D5)Val -> Ile

JP Williams, A Creese, DR Roper, BN Green, Helen Cooper

Research output: Contribution to journalArticlepeer-review

21 Citations (Scopus)
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Abstract

Population migration has led to the global dispersion of human hemoglobinopathies and has precipitated a need for their identification. An effective mass spectrometry-based procedure involves analysis of the intact α- and β-globin chains to determine their mass, followed by location of the variant amino acid residue by direct analysis of the enzymatically digested chains and low-energy collision induced dissociation of the variant peptide. Using this procedure, a variant was identified as either β54Val→Leu or β54Val→Ile, since the amino acids leucine and isoleucine cannot be distinguished using low-energy collisions. Here, we describe how hot electron capture dissociation on a Fourier transform-ion cyclotron resonance mass spectrometer was used to distinguish isoleucine from leucine and identify the mutation as β54(D5)Val→Ile. This is a novel variant, and we have named it Hb Askew.
Original languageEnglish
Pages (from-to)1707-1713
Number of pages7
JournalJournal of the American Society for Mass Spectrometry
Volume20
Issue number9
DOIs
Publication statusPublished - 1 Sept 2009

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