PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 1316115-6 1992 Lactoperoxidase (LPO) could substitute for MPO in the iodide, but not the chloride system. Iodides 54-60 myeloperoxidase Homo sapiens 43-46 16274882-5 2005 The chlorination activity of myeloperoxidase was measured by trapping hypochlorous acid with taurine and subsequently using iodide to promote the oxidation reactions of the accumulated taurine chloramine. Iodides 124-130 myeloperoxidase Homo sapiens 29-44 12612415-0 2003 Modification by fluoride, bromide, iodide, thiocyanate and nitrite anions of reaction of a myeloperoxidase-H2O2-Cl- system with nucleosides. Iodides 35-41 myeloperoxidase Homo sapiens 91-106 9922160-0 1998 Reaction of myeloperoxidase compound I with chloride, bromide, iodide, and thiocyanate. Iodides 63-69 myeloperoxidase Homo sapiens 12-27 9922160-9 1998 SCN- is shown to be most effective in shifting the system myeloperoxidase/hydrogen peroxide from the peroxidatic cycle to the halogenation cycle, whereas iodide is shown to be more effective than bromide which in turn is much more effective than chloride. Iodides 154-160 myeloperoxidase Homo sapiens 58-73 9359420-1 1997 The neutrophil enzyme myeloperoxidase uses H2O2 to oxidize chloride, bromide, iodide and thiocyanate to their respective hypohalous acids. Iodides 78-84 myeloperoxidase Homo sapiens 22-37 8131215-3 1994 Myeloperoxidase-dependent degradation of hyaluronic acid is inhibited by superoxide dismutase, desferrioxamine, iodide ion, bromide ion, mannitol, histidine and various antiinflammatory agents. Iodides 112-118 myeloperoxidase Homo sapiens 0-15 2542309-9 1989 Since as little as 1 atom of iodide bound per molecule of transferrin was associated with substantial losses in iron binding capacity, there appears to be a high specificity of myeloperoxidase-catalyzed iodination for residues at or near the iron binding sites. Iodides 29-35 myeloperoxidase Homo sapiens 177-192 2154520-5 1990 Bromide or iodide caused up to a 7-fold increase in EPO activity and a 1.5-fold increase in MPO activity. Iodides 11-17 myeloperoxidase Homo sapiens 92-95 2154520-10 1990 Stimulation by bromide or iodide could be used to facilitate detection of EPO and to distinguish between MPO and EPO. Iodides 26-32 myeloperoxidase Homo sapiens 105-108 2852626-1 1988 Myeloperoxidase was found to promote peroxidation of phospholipids under acidic conditions in the presence of hydrogen peroxide and iodide ions. Iodides 132-138 myeloperoxidase Homo sapiens 0-15 2425843-6 1986 MA1 and MA3 inhibit MPO activities such as tetraguaiacol formation, iodide oxidation and luminol-dependent chemiluminescence, while MB1 shows no such inhibition. Iodides 68-74 myeloperoxidase Homo sapiens 20-23 2981925-18 1985 Using 125I, we found that exposure of liposomes to the MPO system resulted in an association between iodide and liposomes; moreover, there was a close correspondence between this phenomenon and 51Cr release, suggesting that halogenation may be one mechanism of injury. Iodides 101-107 myeloperoxidase Homo sapiens 55-58 89704-7 1979 On the other hand, 125I incorporation into 131I-DIT was not affected by increased concentrations of MMI up to 10(-5)M. At higher drug concentrations the drug caused inhibition of MPO-catalysed exchange of inorganic iodide for organic iodine in DIT. Iodides 215-221 myeloperoxidase Homo sapiens 179-182 6301581-4 1983 Myeloperoxidase (MPO) in the ID-PMN population showed increased sensitivity to inhibition by 3-amino-1,2,4-triazole, and HD-PMN exhibited a 2-3-fold increase in chloride and iodide oxidation per unit of MPO activity compared to ID-PMN. Iodides 174-180 myeloperoxidase Homo sapiens 0-15 6301581-4 1983 Myeloperoxidase (MPO) in the ID-PMN population showed increased sensitivity to inhibition by 3-amino-1,2,4-triazole, and HD-PMN exhibited a 2-3-fold increase in chloride and iodide oxidation per unit of MPO activity compared to ID-PMN. Iodides 174-180 myeloperoxidase Homo sapiens 17-20 6295926-5 1983 The target cell destruction required the presence of the iodide ion as oxidizable co-factor for the myeloperoxidase-hydrogen peroxide system. Iodides 57-63 myeloperoxidase Homo sapiens 100-115 6266056-4 1981 Using an in vivo model system it has been shown that MPO catalyses the sequential events of iodination, iodine exchange and de-iodination of tyrosines and, furthermore, that all three reactions are influenced by the rate of H2O2 generation and the iodide concentration of the reaction medium. Iodides 248-254 myeloperoxidase Homo sapiens 53-56 6260684-9 1981 A sample of a very highly purified human myeloperoxidase functioned in the presence of hydrogen peroxide and either iodide or chloride to prevent germination of both blastospores and conidiospores. Iodides 116-122 myeloperoxidase Homo sapiens 41-56 211044-2 1978 The neutrophils exhibited a marked decrease in phagocytosis after 1 h. The myeloperoxidase mediated conversion of iodide to a protein-bound form was also decreased. Iodides 114-120 myeloperoxidase Homo sapiens 75-90 225142-2 1978 After phagocytosis, MPO is released into the phagosome from adjacent granules where it interacts with H2O2 generated either by leukocytic or microbial metabolism and a halide such as chloride or iodide to form agents toxic to the ingested organisms. Iodides 195-201 myeloperoxidase Homo sapiens 20-23 4717124-2 1973 Myeloperoxidase, in amounts equivalent to 1.5 x 10(6) neutrophils, readily replaces lactoperoxidase, and allows the substitution of the iodide ion by chloride. Iodides 136-142 myeloperoxidase Homo sapiens 0-15 1173052-1 1975 Erythrocytes are hemolyzed by myeloperoxidase, an H2O2-generating system (glucose + glucose oxidase; hypoxanthine + xanthine oxidase) and an oxidizable cofactor (chloride, iodide, thyroxine, triiodothyronine). Iodides 172-178 myeloperoxidase Homo sapiens 30-45 1120184-4 1975 Myeloperoxidase was effective with either chloride or iodide as the halide, while lastoperoxidase was effective with iodide but not chloride. Iodides 54-60 myeloperoxidase Homo sapiens 0-15 1173052-3 1975 Myeloperoxidase can be replaced by lactoperoxidase in the iodide-, thyroxine and triiodothyronine-dependent, but not in the chloride-dependent, systems. Iodides 58-64 myeloperoxidase Homo sapiens 0-15 4629909-1 1973 Thyroxine (T(4)) and triiodothyronine (T(9)) are rapidly degraded by a purified preparation of myeloperoxidase (MPO) and H(2)O(2) with the formation of iodide and material which remains at the origin on paper chromatography. Iodides 152-158 myeloperoxidase Homo sapiens 95-110 4629909-1 1973 Thyroxine (T(4)) and triiodothyronine (T(9)) are rapidly degraded by a purified preparation of myeloperoxidase (MPO) and H(2)O(2) with the formation of iodide and material which remains at the origin on paper chromatography. Iodides 152-158 myeloperoxidase Homo sapiens 112-115 16557740-4 1970 Since we had previously found that myeloperoxidase (MPO), a lysosomal enzyme of human neutrophils and monocytes, exerted fungicidal activity against Candida albicans when combined with H(2)O(2) and chloride or iodide, the effects of these substances on A. fumigatus spores were examined. Iodides 210-216 myeloperoxidase Homo sapiens 35-50 16557740-4 1970 Since we had previously found that myeloperoxidase (MPO), a lysosomal enzyme of human neutrophils and monocytes, exerted fungicidal activity against Candida albicans when combined with H(2)O(2) and chloride or iodide, the effects of these substances on A. fumigatus spores were examined. Iodides 210-216 myeloperoxidase Homo sapiens 52-55 31568923-0 2020 Iodide modulates protein damage induced by the inflammation-associated heme enzyme myeloperoxidase. Iodides 0-6 myeloperoxidase Homo sapiens 83-98 17359937-5 2007 Compared with wild-type recombinant MPO the cyanide association rate with ferric Met243Val was significantly enhanced as were also the calculated apparent bimolecular compound I reduction rates by iodide (>10(8) M(-1)s(-1)) and thiocyanate (>10(8) M(-1)s(-1)). Iodides 197-203 myeloperoxidase Homo sapiens 36-39