PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 6343501-4 1983 We have modified the buffer by the addition of citric acid and sodium azide to reduce background color development and to inhibit the activity of catalase, respectively. Sodium Azide 63-75 catalase Homo sapiens 146-154 403244-4 1977 Both sodium azide, 8 mM, and 3-amino-1,2,4-triazole, 50 mM, besides inhibiting catalase, inhibited the L-dopa peroxidase activity in each fraction. Sodium Azide 5-17 catalase Homo sapiens 79-87 7139130-3 1982 Erythrocytes from freshly drawn human blood were washed and suspended in isoosmotic phosphate-buffered saline and incubated with sodium azide to inhibit the catalase. Sodium Azide 129-141 catalase Homo sapiens 157-165 194005-4 1977 We have tested this possibility by studying human granulocyte CL in the presence of 0.1 mM sodium azide, a known inhibitor of myeloperoxidase and catalase and a scavenger of 1O2. Sodium Azide 91-103 catalase Homo sapiens 146-154 10917-0 1976 Catalase activates cerebral granylate cyclase in the presence of sodium azide. Sodium Azide 65-77 catalase Homo sapiens 0-8 19778251-6 2009 Catalase inhibition by sodium azide depleted reduced glutathione level further. Sodium Azide 23-35 catalase Homo sapiens 0-8 29753074-3 2018 Fluorescent measurements as well as oxygen production experiments showed that catalase was responsible for most of the decomposition of H2O2 at cell densities suitable for both experimental settings (0.1-10 x 1010 cell L-1), since sodium azide but not N-ethylmaleimide (NEM) inhibited H2O2 consumption. Sodium Azide 231-243 catalase Homo sapiens 78-86 21185058-5 2011 The activity assays were performed in strictly aqueous media and in the presence of increasing concentrations of seven commercially available ionic liquids and sodium azide, a strong inhibitor of catalase. Sodium Azide 160-172 catalase Homo sapiens 196-204 10764744-4 2000 Sodium azide, an inhibitor of catalase, reduced the increased sensitivity of mC5 and C33 cells to TNF-alpha to the level of toxicity found with control Hp cells. Sodium Azide 0-12 catalase Homo sapiens 30-38 23105520-4 2005 Catalase and superoxide dismutase both restored activity by about 18%, mannitol by 13% and sodium azide by 17.3%. Sodium Azide 91-103 catalase Homo sapiens 0-8 11811525-0 2001 Catalase catalyzes nitrotyrosine formation from sodium azide and hydrogen peroxide. Sodium Azide 48-60 catalase Homo sapiens 0-8 11811525-1 2001 Sodium azide (NaN3) is known as an inhibitor of catalase, and a nitric oxide (NO) donor in the presence of catalase and H2O2. Sodium Azide 0-12 catalase Homo sapiens 48-56 11811525-1 2001 Sodium azide (NaN3) is known as an inhibitor of catalase, and a nitric oxide (NO) donor in the presence of catalase and H2O2. Sodium Azide 0-12 catalase Homo sapiens 107-115 11811525-1 2001 Sodium azide (NaN3) is known as an inhibitor of catalase, and a nitric oxide (NO) donor in the presence of catalase and H2O2. Sodium Azide 14-18 catalase Homo sapiens 48-56 11811525-1 2001 Sodium azide (NaN3) is known as an inhibitor of catalase, and a nitric oxide (NO) donor in the presence of catalase and H2O2. Sodium Azide 14-18 catalase Homo sapiens 107-115 11811525-2 2001 We showed here that catalase-catalyzed oxidation of NaN3 can generate reactive nitrogen species which contribute to tyrosine nitration in the presence of H2O2. Sodium Azide 52-56 catalase Homo sapiens 20-28 11811525-3 2001 The formation of free-tyrosine nitration and protein-bound tyrosine nitration by the NaN3/catalase/H2O2 system showed a maximum level at pH 6.0. Sodium Azide 85-89 catalase Homo sapiens 90-98 11811525-8 2001 The generation of nitrite (NO2-) and nitrate (NO3-) by the NaN3/catalase/H2O2 system was maximal at pH 5.0. Sodium Azide 59-63 catalase Homo sapiens 64-72 11811525-9 2001 These results suggested that the oxidation of NaN3 by the catalase/H2O2 system generates unknown peroxynitrite-like reactive nitrogen intermediates, which contribute to tyrosine nitration. Sodium Azide 46-50 catalase Homo sapiens 58-66 16123765-4 2006 The locomotor effects of intranigral ethanol (1.4 micromol) were reduced by coadministration of 10 mg/kg sodium azide, a catalase inhibitor that acts to reduce the metabolism of ethanol into acetaldehyde in the brain. Sodium Azide 105-117 catalase Homo sapiens 121-129 11596115-6 2001 The ability of the catalase inhibitor, sodium azide, to increase the BCNU sensitivity of the bcl-2 transfectants to levels of the BCNU-treated control clone substantiated the role of the catalase activity. Sodium Azide 39-51 catalase Homo sapiens 19-27 11596115-6 2001 The ability of the catalase inhibitor, sodium azide, to increase the BCNU sensitivity of the bcl-2 transfectants to levels of the BCNU-treated control clone substantiated the role of the catalase activity. Sodium Azide 39-51 catalase Homo sapiens 187-195 11506893-2 2001 The capacity of Cp to enhance oxidative damage to DNA was inhibited by hydroxyl radical scavengers such as sodium azide and mannitol, a metal chelator, diethylenetriaminepentaacetic acid, a spin-trapping agent, 5,5-dimethyl-1-pyrroline N-oxide (DMPO) and catalase. Sodium Azide 107-119 catalase Homo sapiens 255-263 10677150-4 2000 RBC were incubated with t-butyl hydroperoxide as an oxidizing agent both in the presence and in the absence of the catalase inhibitor sodium azide. Sodium Azide 134-146 catalase Homo sapiens 115-123 9726283-7 1998 The catalase inhibitors sodium azide and 3-amino-1,2,4-triazole (3-AT) markedly reduced the amount of acetaldehyde produced from 22 mM ethanol in a concentration dependent manner compared with the control samples (0.1 mM sodium azide to 73% and 10 mM 3-AT to 67% of control). Sodium Azide 24-36 catalase Homo sapiens 4-12 10660661-6 2000 Just after exercise, the LgCL response was not affected, while the response of LmCL mixed with sodium azide, which inhibits catalase and myeloperoxidase (MPO) activity, was significantly enhanced (p < 0.05). Sodium Azide 95-107 catalase Homo sapiens 124-132 9726283-7 1998 The catalase inhibitors sodium azide and 3-amino-1,2,4-triazole (3-AT) markedly reduced the amount of acetaldehyde produced from 22 mM ethanol in a concentration dependent manner compared with the control samples (0.1 mM sodium azide to 73% and 10 mM 3-AT to 67% of control). Sodium Azide 221-233 catalase Homo sapiens 4-12 9557922-4 1998 METHODS: An electrode technique was used to determine plasma hydrogen peroxide levels after blockade of endogenous catalase with sodium azide. Sodium Azide 129-141 catalase Homo sapiens 115-123 1416429-5 1992 Serum H2O2 scavenging activity correlated with serum catalase (r = 0.77) but not GPX (r = 0.33) activity and was inhibitable (greater than 90%) by sodium azide, a catalase inhibitor. Sodium Azide 147-159 catalase Homo sapiens 53-61 8593088-1 1995 When tetracycline and chlortetracycline were incubated an a dark room in the presence of erythrocytes with erythrocytic catalase completely inactivated by sodium azide, the antibiotics induced methemoglobin formation in them. Sodium Azide 155-167 catalase Homo sapiens 120-128 9025968-6 1997 Addition of the catalase inhibitor NaN3 completely inhibits H2O2 decomposition. Sodium Azide 35-39 catalase Homo sapiens 16-24 8389671-7 1993 The H2O2 decomposing activity was almost completely inhibited by sodium azide (NaN3) or aminotriazole, both catalase inhibitors. Sodium Azide 65-77 catalase Homo sapiens 108-116 8389671-7 1993 The H2O2 decomposing activity was almost completely inhibited by sodium azide (NaN3) or aminotriazole, both catalase inhibitors. Sodium Azide 79-83 catalase Homo sapiens 108-116 1319369-4 1992 In ulcerative colitis, luminol chemiluminescence correlated with microscopic inflammation (Spearman"s p = 0.74, P = 0.0001) and was decreased by sodium azide (-89%, P less than 0.05), taurine (-31%, P less than 0.05), catalase (-23%, P less than 0.05), and dimethyl sulfoxide (-29%, P less than 0.05). Sodium Azide 145-157 catalase Homo sapiens 218-226 2029741-4 1991 Sodium azide, an inhibitor of myeloperoxidase and catalase, reduced the nitrite-stimulated metabolism of BP-7,8-diol in PMA-activated leukocytes. Sodium Azide 0-12 catalase Homo sapiens 50-58 3239759-11 1988 Catalase of muscle was inhibited 50% by 2 microM sodium azide. Sodium Azide 49-61 catalase Homo sapiens 0-8 1801700-3 1991 Both H2O2 (5 mM) and glucose oxidase (0.2 U/ml) decreased by 82-88% rates of proteolysis only in skeletal muscles pretreated with sodium azide (0.25 mM) to inactivate endogenous catalase. Sodium Azide 130-142 catalase Homo sapiens 178-186 2830916-6 1987 Using the OH-radical scavengers (mannitol, N-butanol, alpha-naphthol) and the catalase inhibitor sodium azide, it was shown that the OH-radical participates in microsomal oxidation of DCNQ and aminopyrine. Sodium Azide 97-109 catalase Homo sapiens 78-86