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It seems that the enzymatic complex of catalasemyeloperoxidase is consuming most of the hydrogen peroxide, which can no longer interact with ionic iron or oxygen.[] More than that, most of the ionic iron is preserved in the cell chelated to proteins (transferring, lactoferrin, and ferritin).[] Apart from its reducing potential, myeloperoxidase seems to have oxidation potential for chloride ions by hydrogen peroxide yielding a highly cytotoxic neutrophil system.[] It has been also shown that hypochlorous acid is much more toxic than common ROS and can easily react with sulfhydryl, amino acids, nitrogenous compounds, pyridine nucleotides, but not with peroxide polyunsaturated lipids.[] Furthermore, the N -chloramine products contain oxidizing equivalents too, also toxic and extremely instable, influencing membrane permeability.[] They can also interact with intracellular compounds resulting in chloramine, which is significantly more toxic than hypochlorous acid for bacteria and certain eukaryotic cells.[] These suggest that neutrophil oxidants may be important in the pathogenesis of the depressed intestinal contractility mechanism

Research Interest Researchers often explore peptides because they can influence biological signaling pathways

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