Alternative LC/ESI-MS/MS approach to screen hemoglobin N-terminal modifications

研究成果: Article査読

抄録

Proteins are continuously exposed to reactive chemical species owing to physiological and chemical stresses, resulting in various chemical modifications such as oxidation, nitration, glycation/glycoxidation, lipidation/lipoxidation, and adduct formation with drugs/chemicals. Hemoglobin (Hb) is the most abundant protein in blood (∼150 mg/mL) with a long half-life (turnover: 126 days). Hb is thus believed to be a major target of reactive chemical species and those modifications reflect biological events. Chemical modifications on Hb have been analyzed as N-terminal valine (Val) adducts by the Edman degradation reaction because Val is the N-terminal amino acid in both the α- and β-subunits of Hb and is exposed on the surface of the protein. However, this strategy is limited to N-terminal alkylated Val and overlooks N-terminal acylated and deaminated Val. Here, we describe a proof-of-concept study to develop an alternative screening approach based on liquid chromatography-tandem mass spectrometry with peptide-specific constant neutral loss/precursor ion scanning to include all types of N-terminal modifications on Hb.

本文言語English
論文番号116651
ジャーナルInternational Journal of Mass Spectrometry
468
DOI
出版ステータスPublished - 2021 10

ASJC Scopus subject areas

  • 器械工学
  • 凝縮系物理学
  • 分光学
  • 物理化学および理論化学

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