Antimicrobial Activity of Myeloperoxidase from Neutrophilic Peroxisome |
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| Authors: | P G But R A Murav'ev V A Fomina V V Rogovin |
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| Institution: | (1) Semenov Institute of Chemical Physics, Russian Academy of Sciences, ul. Kosygina 4, Moscow, 119991, Russia |
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| Abstract: | Myeloperoxidase plays the key role in antimicrobial oxygen-dependent activity of neutrophils. This heme-containing enzyme catalyzes HOCl formation from H2O2 and Cl–. HOCl is a strong oxidation agent produced at the significant level by neutrophils. Myeloperoxidase easily oxidizes thiocyanate to hypothiocyanate and Br– to HOBr, which are involved in protective reactions. Myeloperoxidase reacts quickly with nitric oxide and peroxynitrite in inflammation foci. All these reactions affect neutrophil-induced oxidative stress. |
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