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- W2022341306 abstract "N-carbamoylation is the non-enzymatic reaction of cyanate with amino groups. Due to urea-formed cyanate in uremic patients beside carbamoylated proteins also free amino acid carbamoylation has been detected, a modification which has been linked to disturbed protein synthesis as NH2-derivatisation interferes with peptide bond formation. HOCl the product of the activated MPO/H2O2/Cl− system is known to react with the NH2-group of free amino acids to form chloramines which could exert some protective effect against protein modification and cytotoxicity induced by HOCl. As N-carbamoylation may inhibit formation of chloramines we have used N-carbamoyl-threonine as a model amino acid to study its ability to limit the reactivity of HOCl with proteins (LDL and human serum albumin) and cells (THP-1 monocytes and coronary artery endothelial cells). The data indicate that N-carbamoylation completely abolished the protein- and cell-protective effect of threonine against HOCl attack. In contrast to threonine the reaction of HOCl with carbamoyl-threonine resulted in the formation of volatile oxidant species with protein modifying and cytotoxic potential. The volatile lipophilic inorganic monochloramine (NH2Cl) was identified as a breakdown product of this reaction." @default.
- W2022341306 created "2016-06-24" @default.
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- W2022341306 date "2012-11-01" @default.
- W2022341306 modified "2023-10-17" @default.
- W2022341306 title "Carbamoylated free amino acids in uremia: HOCl generates volatile protein modifying and cytotoxic oxidant species from N-carbamoyl-threonine but not threonine" @default.
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- W2022341306 doi "https://doi.org/10.1016/j.biochi.2012.06.032" @default.
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