PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15736921-7 2004 Moreover, the extracts inhibited MPO-catalyzed guaiacol oxidation in a concentration-dependent manner in a cell-free assay but, in contrast, did not affect MPO activity in isolated human neutrophils. Guaiacol 47-55 myeloperoxidase Homo sapiens 33-36 18819272-4 2008 The inhibitor of myeloperoxidase NaN3, the HOCl scavengers taurine and methionine, and guaiacol, a substrate for peroxidation cycle of myeloperoxidase, prevented luminescence. Guaiacol 87-95 myeloperoxidase Homo sapiens 135-150 18237554-2 2008 DESIGN AND METHODS: The assay system employs a novel sensitive substrate from 3,3"-diaminobenzidine (DAB) and guaiacol in the presence of dapsone (4,4"-diaminodiphenylsulfone) to determine MPO activity in whole saliva using an original "sandwich" test-disk (DEAE-cellulose paper and cellulose chromatography paper). Guaiacol 110-118 myeloperoxidase Homo sapiens 189-192 12711384-3 2003 According to our results, when 50% of the peroxidase activity in saliva was due to MPO, determined using a typical substrate for peroxidase guaiacol, almost all oxygen evolved was due to SPX. Guaiacol 140-148 myeloperoxidase Homo sapiens 83-86 1964765-4 1990 Regression equations have been determined which can be used to calculate concentrations of bovine lactoperoxidase (LPO), human salivary peroxidase (SPO), and human myeloperoxidase (MPO) from activities measured with the following donors: pyrogallol, guaiacol, 2,2"-azinobis(3-ethylbenzylthiazoline-6-sulfonic acid), and thiocyanate (SCN-). Guaiacol 250-258 myeloperoxidase Homo sapiens 181-184 8001699-8 1994 Using H2O2 as substrate and guaiacol as an electron acceptor, the enzyme activity of crude enzyme extract derived from broken hemocytes was analyzed; enzyme activity similar to that of human myeloperoxidase (MPO) (0.104 U/mg protein) was observed. Guaiacol 28-36 myeloperoxidase Homo sapiens 191-206 8001699-8 1994 Using H2O2 as substrate and guaiacol as an electron acceptor, the enzyme activity of crude enzyme extract derived from broken hemocytes was analyzed; enzyme activity similar to that of human myeloperoxidase (MPO) (0.104 U/mg protein) was observed. Guaiacol 28-36 myeloperoxidase Homo sapiens 208-211 1849156-2 1991 The guaiacol assay, for example, which is one of the most commonly used assays for peroxidase activity, is sensitive to both eosinophil peroxidase (EPO) and the peroxidase of neutrophils, i.e., myeloperoxidase (MPO), thus preventing distinction of the two peroxidases in mixed neutrophil-eosinophil populations. Guaiacol 4-12 myeloperoxidase Homo sapiens 194-209 1849156-2 1991 The guaiacol assay, for example, which is one of the most commonly used assays for peroxidase activity, is sensitive to both eosinophil peroxidase (EPO) and the peroxidase of neutrophils, i.e., myeloperoxidase (MPO), thus preventing distinction of the two peroxidases in mixed neutrophil-eosinophil populations. Guaiacol 4-12 myeloperoxidase Homo sapiens 211-214 1847381-5 1991 Salicylhydroxamic acid serves as a donor to the higher oxidation state of myeloperoxidase and thereby inhibits guaiacol oxidation. Guaiacol 111-119 myeloperoxidase Homo sapiens 74-89 9820817-0 1998 Oxidation of guaiacol by myeloperoxidase: a two-electron-oxidized guaiacol transient species as a mediator of NADPH oxidation. Guaiacol 13-21 myeloperoxidase Homo sapiens 25-40 9820817-0 1998 Oxidation of guaiacol by myeloperoxidase: a two-electron-oxidized guaiacol transient species as a mediator of NADPH oxidation. Guaiacol 66-74 myeloperoxidase Homo sapiens 25-40 9820817-1 1998 The present study was first aimed at a complete steady-state kinetic analysis of the reaction between guaiacol (2-methoxyphenol) and the myeloperoxidase (MPO)/H2O2 system, including a description of the isolation and purification of MPO from human polymorphonuclear neutrophil cells. Guaiacol 102-110 myeloperoxidase Homo sapiens 137-152 9820817-1 1998 The present study was first aimed at a complete steady-state kinetic analysis of the reaction between guaiacol (2-methoxyphenol) and the myeloperoxidase (MPO)/H2O2 system, including a description of the isolation and purification of MPO from human polymorphonuclear neutrophil cells. Guaiacol 102-110 myeloperoxidase Homo sapiens 154-157 9820817-1 1998 The present study was first aimed at a complete steady-state kinetic analysis of the reaction between guaiacol (2-methoxyphenol) and the myeloperoxidase (MPO)/H2O2 system, including a description of the isolation and purification of MPO from human polymorphonuclear neutrophil cells. Guaiacol 102-110 myeloperoxidase Homo sapiens 233-236 9820817-1 1998 The present study was first aimed at a complete steady-state kinetic analysis of the reaction between guaiacol (2-methoxyphenol) and the myeloperoxidase (MPO)/H2O2 system, including a description of the isolation and purification of MPO from human polymorphonuclear neutrophil cells. Guaiacol 112-127 myeloperoxidase Homo sapiens 137-152 9820817-1 1998 The present study was first aimed at a complete steady-state kinetic analysis of the reaction between guaiacol (2-methoxyphenol) and the myeloperoxidase (MPO)/H2O2 system, including a description of the isolation and purification of MPO from human polymorphonuclear neutrophil cells. Guaiacol 112-127 myeloperoxidase Homo sapiens 154-157 9820817-1 1998 The present study was first aimed at a complete steady-state kinetic analysis of the reaction between guaiacol (2-methoxyphenol) and the myeloperoxidase (MPO)/H2O2 system, including a description of the isolation and purification of MPO from human polymorphonuclear neutrophil cells. Guaiacol 112-127 myeloperoxidase Homo sapiens 233-236 9820817-2 1998 Secondly, the overall reaction of the oxidation of NADPH, mediated by the reactive intermediates formed from the oxidation of guaiacol in the MPO/H2O2 system, was analysed kinetically. Guaiacol 126-134 myeloperoxidase Homo sapiens 142-145 9820817-3 1998 The presence of guaiacol stimulates the oxidation of NADPH by the MPO/H2O2 system in a concentration-dependent manner. Guaiacol 16-24 myeloperoxidase Homo sapiens 66-69 9820817-5 1998 Under these conditions, the stoichiometry of NADPH:H2O2 is 1, and the oxidation rate of NADPH approximates to that of the rate of guaiacol oxidation by MPO. Guaiacol 130-138 myeloperoxidase Homo sapiens 152-155 3032796-9 1987 MPO bound to the high-avidity sites did not oxidize guaiacol but oxidized chloride, as detected by the chlorination of taurine. Guaiacol 52-60 myeloperoxidase Homo sapiens 0-3 2153031-4 1990 First, we measured respective enzymatic activity using a panel of substrates; MPO I was found to have lower activity with some substrates (pyrogallol, guaiacol, potassium iodide [KI]), but similar activity to the other isoenzymes with 4-aminoantipyrine. Guaiacol 151-159 myeloperoxidase Homo sapiens 78-81 2542140-3 1989 Also, conjugated bilirubin and its metabolic precursor, biliverdin, do not inhibit the enzyme myeloperoxidase (MPO) since (i) the MPO-dependent oxidation of guaiacol is not affected by biliverdin and (ii) the spectral changes observed when conjugated bilirubin is oxidized by a MPO-H2O2-Cl(-)-system are very similar to those obtained with reagent HOCl. Guaiacol 157-165 myeloperoxidase Homo sapiens 130-133 2542140-3 1989 Also, conjugated bilirubin and its metabolic precursor, biliverdin, do not inhibit the enzyme myeloperoxidase (MPO) since (i) the MPO-dependent oxidation of guaiacol is not affected by biliverdin and (ii) the spectral changes observed when conjugated bilirubin is oxidized by a MPO-H2O2-Cl(-)-system are very similar to those obtained with reagent HOCl. Guaiacol 157-165 myeloperoxidase Homo sapiens 130-133 31769316-0 2020 Methoxyphenol derivatives as reversible inhibitors of myeloperoxidase as potential antiatherosclerotic agents. Guaiacol 0-13 myeloperoxidase Homo sapiens 54-69 6284284-1 1982 Family studies on myeloperoxidase (MPO) deficiency have been carried out by quantitating the peroxidase activity of granulocyte preparations with three methods, namely guaiacol peroxidation, alanine decarboxylation, and spectroscopic analysis. Guaiacol 168-176 myeloperoxidase Homo sapiens 18-33 6284284-1 1982 Family studies on myeloperoxidase (MPO) deficiency have been carried out by quantitating the peroxidase activity of granulocyte preparations with three methods, namely guaiacol peroxidation, alanine decarboxylation, and spectroscopic analysis. Guaiacol 168-176 myeloperoxidase Homo sapiens 35-38 206633-3 1978 MPO adsorbed onto the bacterial surface is not accessible to other competing substrates such as guaiacol and [1(-14)C] alanine. Guaiacol 96-104 myeloperoxidase Homo sapiens 0-3 2821929-2 1987 MPO catalyzes the oxidation of guaiacol into tetraguaiacol in the presence of H2O2. Guaiacol 31-39 myeloperoxidase Homo sapiens 0-3 6280744-5 1982 Eosinophil peroxidase, which is present in MPO deficient subjects, interfered with the guaiacol assay of MPO, and in several cases masked the genetic transmission. Guaiacol 87-95 myeloperoxidase Homo sapiens 105-108 229574-4 1979 Guaiacol also inhibited myeloperoxidase-catalysed iodination, and its iodination inhibition curve was nearly identical to that obtained with the anti-inflammatory drugs. Guaiacol 0-8 myeloperoxidase Homo sapiens 24-39 32368837-0 2020 Discovery of novel synthetic hydroxyanisole derivatives as promising myeloperoxidase inhibitors (MPOIs) targeting atherosclerotic CVD. Guaiacol 29-43 myeloperoxidase Homo sapiens 69-84