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Investigation of sarin(Se) reactivity against human plasma proteins using liquid chromatography–tandem mass spectrometry
Author(s) -
Saeidian Hamid,
Hosseini Seyed Esmaeil,
Amoozadeh Ali,
Naseri Mohammad Taghi,
Babri Mehran
Publication year - 2018
Publication title -
journal of mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 1076-5174
DOI - 10.1002/jms.4045
Subject(s) - sarin , chemistry , chromatography , mass spectrometry , nerve agent , tandem mass spectrometry , butyrylcholinesterase , liquid chromatography–mass spectrometry , paraoxon , organic chemistry , acetylcholinesterase , enzyme , aché
Electron ionization mass spectrum of sarin(Se) was interpreted in compare of sarin MS spectrum. Inhibition of butyrylcholinesterase of human plasma by sarin and sarin(Se) was determined spectrophotometrically using modified Ellman method. It appeared that after incubation with sarin and sarin(Se), cholinesterase inhibition were 93% and 83%, respectively. Sarin, sarin(Se), and sarin(Se)‐d 7 were spiked into a vial containing human plasma, and albumin adduct metabolites were identified using liquid chromatography–tandem mass spectrometry. The experiments show that these agents are attached to tyrosine on albumin in human blood. Corresponding deuterated adducts were used to confirm the proposed mechanisms for the formation of the fragments in mass spectrometry experiments.