PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 22434701-3 2012 The products of nitrite (NO(2) (-) ) oxidation by salivary peroxidase (SPO) and commercial bovine lactoperoxidase (LPO) are studied by utilizing an electrochemical assay that allows the direct, continuous monitoring of NO and/or NO(2) and by HPLC to assess nitrates at the end of the reaction. Nitrites 16-23 lactoperoxidase Homo sapiens 50-69 17250799-4 2007 The pseudoperoxidase activity of lactoperoxidase increased lipid peroxidation, while thiocyanate and nitrite-reduced lipid peroxidation. Nitrites 101-108 lactoperoxidase Homo sapiens 33-48 10218656-3 1999 While LPO/H2O2 alone generated only minute amounts of radicals from these compounds, the yield of radicals increased sharply when nitrite was also present. Nitrites 130-137 lactoperoxidase Homo sapiens 6-9 12878034-7 2003 The biological implication of drug activation by LPO with nitrite is discussed. Nitrites 58-65 lactoperoxidase Homo sapiens 49-52 11389723-0 2001 Mechanism of nitrite-stimulated catalysis by lactoperoxidase. Nitrites 13-20 lactoperoxidase Homo sapiens 45-60 11389723-1 2001 The reactions of lactoperoxidase (LPO) intermediates compound I, compound II and compound III, with nitrite (NO2(-)) were investigated. Nitrites 100-107 lactoperoxidase Homo sapiens 17-32 11389723-1 2001 The reactions of lactoperoxidase (LPO) intermediates compound I, compound II and compound III, with nitrite (NO2(-)) were investigated. Nitrites 100-107 lactoperoxidase Homo sapiens 34-37 12971945-0 2003 Human salivary peroxidase-catalyzed oxidation of nitrite and nitration of salivary components 4-hydroxyphenylacetic acid and proteins. Nitrites 49-56 lactoperoxidase Homo sapiens 6-25 12971945-3 2003 H2O2-dependent oxidation of nitrite and H2O2-dependent nitration of HPA were observed in dialyzed saliva and by partially purified salivary peroxidase (SPX). Nitrites 28-35 lactoperoxidase Homo sapiens 131-150 12971945-3 2003 H2O2-dependent oxidation of nitrite and H2O2-dependent nitration of HPA were observed in dialyzed saliva and by partially purified salivary peroxidase (SPX). Nitrites 28-35 lactoperoxidase Homo sapiens 152-155 10218656-0 1999 Oxidation of biological electron donors and antioxidants by a reactive lactoperoxidase metabolite from nitrite (NO2-): an EPR and spin trapping study. Nitrites 103-110 lactoperoxidase Homo sapiens 71-86 10218656-1 1999 We report that a lactoperoxidase (LPO) metabolite derived from nitrite (NO2-) catalyses one-electron oxidation of biological electron donors and antioxidants such as NADH, NADPH, cysteine, glutathione, ascorbate, and Trolox C. Nitrites 63-70 lactoperoxidase Homo sapiens 17-32 10218656-1 1999 We report that a lactoperoxidase (LPO) metabolite derived from nitrite (NO2-) catalyses one-electron oxidation of biological electron donors and antioxidants such as NADH, NADPH, cysteine, glutathione, ascorbate, and Trolox C. Nitrites 63-70 lactoperoxidase Homo sapiens 34-37 10218656-4 1999 In aerated buffer (pH 7) the nitrite-dependent oxidation of NAD(P)H by LPO/H2O2 produced superoxide radical, O2*-, which was detected as a DMPO/*O2H adduct. Nitrites 29-36 lactoperoxidase Homo sapiens 71-74 10218656-5 1999 We propose that in the LPO/H2O2/NO2-/biological electron donor systems the nitrite functions as a catalyst because of its preferential oxidation by LPO to a strongly oxidizing metabolite, most likely a nitrogen dioxide radical *NO2, which then reacts with the biological substrates more efficiently than does LPO/H2O2 alone. Nitrites 75-82 lactoperoxidase Homo sapiens 23-26 10218656-5 1999 We propose that in the LPO/H2O2/NO2-/biological electron donor systems the nitrite functions as a catalyst because of its preferential oxidation by LPO to a strongly oxidizing metabolite, most likely a nitrogen dioxide radical *NO2, which then reacts with the biological substrates more efficiently than does LPO/H2O2 alone. Nitrites 75-82 lactoperoxidase Homo sapiens 148-151 10218656-5 1999 We propose that in the LPO/H2O2/NO2-/biological electron donor systems the nitrite functions as a catalyst because of its preferential oxidation by LPO to a strongly oxidizing metabolite, most likely a nitrogen dioxide radical *NO2, which then reacts with the biological substrates more efficiently than does LPO/H2O2 alone. Nitrites 75-82 lactoperoxidase Homo sapiens 148-151 9667498-6 1998 We propose that the mechanism for the generation of melanin radicals by the LPO/H2O2/nitrite system involves oxidation of NO2- by LPO/H2O2 to a reactive metabolite, most likely the nitrogen dioxide radical (.NO2), which subsequently reacts with melanin 5,6-dihydroxyindole subunits producing the respective semiquinone radicals. Nitrites 85-92 lactoperoxidase Homo sapiens 76-79 9667498-0 1998 Lactoperoxidase-catalyzed oxidation of melanin by reactive nitrogen species derived from nitrite (NO2-): an EPR study. Nitrites 89-96 lactoperoxidase Homo sapiens 0-15 9667498-2 1998 We observed that in the presence of nitrite LPO/H2O2 generated large amount of melanin radicals, as evidenced by a strong, up to 11-fold, increase in the intensity of the melanin EPR signal. Nitrites 36-43 lactoperoxidase Homo sapiens 44-47 9667498-5 1998 When the nitrite was present, the concentration of melanin radicals was linearly dependent on [NO2-] (for [NO2-] <5 mM), and increased when [LPO] and [H2O2] increased (at constant [NO2-]). Nitrites 9-16 lactoperoxidase Homo sapiens 144-147 9667498-6 1998 We propose that the mechanism for the generation of melanin radicals by the LPO/H2O2/nitrite system involves oxidation of NO2- by LPO/H2O2 to a reactive metabolite, most likely the nitrogen dioxide radical (.NO2), which subsequently reacts with melanin 5,6-dihydroxyindole subunits producing the respective semiquinone radicals. Nitrites 85-92 lactoperoxidase Homo sapiens 130-133 9437521-4 1997 Here we report that in the presence of nitrite ions (NO2-), MXH2 undergoes oxidation by the mammalian enzyme lactoperoxidase (LPO) and hydrogen peroxide and that the process proceeds at a rate that is proportional to NO2- concentration. Nitrites 39-46 lactoperoxidase Homo sapiens 109-124 9437521-4 1997 Here we report that in the presence of nitrite ions (NO2-), MXH2 undergoes oxidation by the mammalian enzyme lactoperoxidase (LPO) and hydrogen peroxide and that the process proceeds at a rate that is proportional to NO2- concentration. Nitrites 39-46 lactoperoxidase Homo sapiens 126-129 7769383-7 1995 The low-spin component of the spectrum has been assigned to an LPO-NO2- adduct due to the presence of some nitrite impurities originating either from commercial unpasteurized milk or from external sources. Nitrites 107-114 lactoperoxidase Homo sapiens 63-66