An LC/ESI-SRM/MS method to screen chemically modified hemoglobin: simultaneous analysis for oxidized, nitrated, lipidated, and glycated sites

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4 Citations (Scopus)

Abstract

Proteins are continuously exposed to various reactive chemical species (reactive oxygen/nitrogen species, endogenous/exogenous aldehydes/epoxides, etc.) due to physiological and chemical stresses, resulting in various chemical modifications such as oxidation, nitration, glycation/glycoxidation, lipidation/lipoxidation, and adduct formation with drugs/chemicals. Abundant proteins with a long half-life, such as hemoglobin (Hb, t1/2 63 days, ∼150 mg/mL), are believed to be major targets of reactive chemical species that reflect biological events. Chemical modifications on Hb have been investigated mainly by mechanistic in vitro experiments or in vivo/clinical experiments focused on single target modifications. Here, we describe an optimized LC/ESI-SRM/MS method to screen oxidized, nitrated, lipidated, and glycated sites on Hb. In vivo preliminary results suggest that this method can detect simultaneously the presence of oxidation (+16 Da) of α-Met32, α-Met76, β-Met55, and β-Trp15 and adducts of malondialdehyde (+54 Da) and glycation (+162 Da) of β-Val1 in a blood sample from a healthy volunteer. [Figure not available: see fulltext.]

Original languageEnglish
Pages (from-to)5379-5392
Number of pages14
JournalAnalytical and Bioanalytical Chemistry
Volume408
Issue number19
DOIs
Publication statusPublished - 2016 Jul 1

Keywords

  • Chemical modification
  • Hemoglobin
  • Mass spectrometry
  • Proteomics

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry

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