A possible origin of chemiluminsecence in phagocytosing neutrophils. Myeloperoxidase-mediated chlorination of proteins and tryptophan |
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Authors: | J M Zgliczyński E Olszowska S Olszowski T Stelmaszyńska E Kwasnowska |
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Institution: | 1. Key Laboratory of Functional Small Organic Molecule, Ministry of Education and College of Life Science, Jiangxi Normal University, 99 Ziyang Road, Nanchang, Jiangxi 330022, China;2. Key Laboratory of Green Chemistry, Jiangxi Province and College of Chemistry and Chemical Engineering, Jiangxi Normal University, 99 Ziyang Road, Nanchang, Jiangxi, 330022, China |
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Abstract: | Chlorination of proteins by the myeloperoxidase-H2O2-Cl- system results in light emission. Out of all amino acids present in proteins only tryptophan delivers light during chlorination. Chlorination of tryptophan by the myeloperoxidase-H2O2-Cl- system, as well as by HOCl or taurine chloramine is associated with chemiluminescence. pH dependence and time pattern of light emission is similar for chlorination of tryptophan by the myeloperoxidase system and taurine, but appears to be different for chlorination by HOCl. Aerobic conditions are necessary for chemiluminescence of chlorinated tryptophan. |
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