Summary.
It has been reported, that sulphoacetalhehyde is formed in the fagocytozing PMNs and its production is taurine monochloramine mediated. Since H2O2 and secreted MPO are present in the medium the non- and enzymatic peroxidation of taurine of its mono- and dichloramines were examined within the pH range 5.3–7.4. The formation of sulphoacetaldehyde was observed in nonenzymatic hydrolysis of taurine N,N-dichloramine (pH 5.3) as well as for monochloramine at pH 7.4. It was found also that its formation was accelerated in the presence of H2O2, in the MPO/H2O2 and in the full system containing Cl−. Additionally it was shown that also horseradish peroxidase (HRP) could catalyze sulphoacetaldehyde production. The sulphoacetaldehyde formation in the examined systems was confirmed with the use of 1HNMR spectra of separated 2,4-dinitrophenylhydrazone derivative. Our results suggest that both non- and ezymatic processes could contribute to the sulphoacetaldehyde formation at site of inflammation.
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Received May 14, 2001 Accepted July 26, 2001
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Olszowski, S., Olszowska, E., Kusior, D. et al. Sulphoacetaldehyde as a product of taurine chloramine peroxidation at site of inflammation. Amino Acids 22, 145–153 (2002). https://doi.org/10.1007/s007260200003
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DOI: https://doi.org/10.1007/s007260200003