PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 32575551-2 2020 Catalase is an antioxidant enzyme that plays a significant role in cellular protection against oxidative damage by the degradation of hydrogen peroxide to oxygen and water. Hydrogen Peroxide 134-151 catalase Bos taurus 0-8 32828412-7 2020 Calves produced using IVF had a greater activity of catalase and glutathione peroxidase, either due to greater production of hydrogen peroxide or greater efficiency of enzymatic response of these neonates. Hydrogen Peroxide 125-142 catalase Bos taurus 52-60 29573798-11 2018 Compared with the control, cells transfected with NFE2L2-siRNA3 with or without H2O2 had lower production of ROS and MDA and activity of SOD, CAT, GSH-Px, and GST. Hydrogen Peroxide 80-84 catalase Bos taurus 142-145 32329223-5 2020 As hydrogen peroxide is rapidly cleared by erythrocytic catalase and glutathione peroxidase, sulfo-cyanine 7, HRP, and lactate oxidase are encapsulated in a liposomal reaction compartment. Hydrogen Peroxide 3-20 catalase Bos taurus 56-64 23316810-3 2013 Immobilized catalase showed the maximal enzyme activity at pH 7.0 at 30 C. The kinetic parameters, Km and Vmax, for immobilized catalase on alanine-chitosan beads and lysine-chitosan beads were estimated to be 25.67 mM, 27 mM and 201.39 mumol H2O2/min, 197.50 mumol H2O2/min, respectively. Hydrogen Peroxide 243-247 catalase Bos taurus 12-20 23249140-1 2013 Catalase is an important antioxidant enzyme that catalyzes the disproportionation of H2O2 into harmless water and molecular oxygen. Hydrogen Peroxide 85-89 catalase Bos taurus 0-8 23316810-3 2013 Immobilized catalase showed the maximal enzyme activity at pH 7.0 at 30 C. The kinetic parameters, Km and Vmax, for immobilized catalase on alanine-chitosan beads and lysine-chitosan beads were estimated to be 25.67 mM, 27 mM and 201.39 mumol H2O2/min, 197.50 mumol H2O2/min, respectively. Hydrogen Peroxide 243-247 catalase Bos taurus 128-136 23316810-3 2013 Immobilized catalase showed the maximal enzyme activity at pH 7.0 at 30 C. The kinetic parameters, Km and Vmax, for immobilized catalase on alanine-chitosan beads and lysine-chitosan beads were estimated to be 25.67 mM, 27 mM and 201.39 mumol H2O2/min, 197.50 mumol H2O2/min, respectively. Hydrogen Peroxide 266-270 catalase Bos taurus 12-20 23316810-3 2013 Immobilized catalase showed the maximal enzyme activity at pH 7.0 at 30 C. The kinetic parameters, Km and Vmax, for immobilized catalase on alanine-chitosan beads and lysine-chitosan beads were estimated to be 25.67 mM, 27 mM and 201.39 mumol H2O2/min, 197.50 mumol H2O2/min, respectively. Hydrogen Peroxide 266-270 catalase Bos taurus 128-136 22565543-0 2012 Kinetics of hydrogen peroxide decomposition by catalase: hydroxylic solvent effects. Hydrogen Peroxide 12-29 catalase Bos taurus 47-55 21541840-5 2011 Therefore, an attempt has been made to predict the structure of the crab catalase and to envisage its catalytic interaction with H(2)O(2). Hydrogen Peroxide 129-137 catalase Bos taurus 73-81 21529340-5 2011 Therefore, the objective of this work was to investigate the contribution of the solvent molecules on the catalytic reaction of bovine liver catalase with its substrate H2O2 by the osmotic stress method. Hydrogen Peroxide 169-173 catalase Bos taurus 141-149 21541840-8 2011 Molecular docking has been used to know the binding modes of hydrogen peroxide with the crab catalase protein. Hydrogen Peroxide 61-78 catalase Bos taurus 93-101 21541840-10 2011 The docking results showed that the three important determinant residues Arg68, Val70 and Arg108 in catalase were binding with H(2)O(2) as they had strong hydrogen bonding contacts with the substrate. Hydrogen Peroxide 127-135 catalase Bos taurus 100-108 18050914-1 2007 The co-immobilization of Aspergillus niger glucose oxidase (GOD) with bovine liver catalase (CAT) onto florisil (magnesium silicate-based porous carrier) was investigated to improve the catalytic efficiency of GOD against H2O2 inactivation. Hydrogen Peroxide 222-226 catalase Bos taurus 83-91 21314602-0 2010 Catalase activity of cytochrome C oxidase assayed with hydrogen peroxide-sensitive electrode microsensor. Hydrogen Peroxide 55-72 catalase Bos taurus 0-8 21314602-3 2010 The catalase (or, rather, pseudocatalase) activity of bovine cytochrome oxidase is characterized by a second order rate constant of ~2 10(2) M(-1) sec(-1) at pH 7.0 and room temperature, which, when divided by the number of H2O2 molecules disappearing in one catalytic turnover (between 2 and 3), agrees reasonably well with the second order rate constant for H2O2-dependent conversion of the oxidase intermediate F(I)-607 to F(II)-580. Hydrogen Peroxide 224-228 catalase Bos taurus 4-12 21314602-3 2010 The catalase (or, rather, pseudocatalase) activity of bovine cytochrome oxidase is characterized by a second order rate constant of ~2 10(2) M(-1) sec(-1) at pH 7.0 and room temperature, which, when divided by the number of H2O2 molecules disappearing in one catalytic turnover (between 2 and 3), agrees reasonably well with the second order rate constant for H2O2-dependent conversion of the oxidase intermediate F(I)-607 to F(II)-580. Hydrogen Peroxide 360-364 catalase Bos taurus 4-12 21314602-4 2010 Accordingly, the catalase activity of bovine oxidase may be explained by H2O2 procession in the oxygen-reducing center of the enzyme yielding superoxide radicals. Hydrogen Peroxide 73-77 catalase Bos taurus 17-25 18050914-1 2007 The co-immobilization of Aspergillus niger glucose oxidase (GOD) with bovine liver catalase (CAT) onto florisil (magnesium silicate-based porous carrier) was investigated to improve the catalytic efficiency of GOD against H2O2 inactivation. Hydrogen Peroxide 222-226 catalase Bos taurus 93-96 18050914-7 2007 The storage stability of the co-immobilized GOD-CAT was also found to be higher than that of the free form at both 5 degrees C and 25 degrees C. The increased GOD activity and reusability resulting from the co-immobilization process may have been due to CAT protecting GOD from inactivation by H2O2 and supplying additional O2 to the reaction system. Hydrogen Peroxide 294-298 catalase Bos taurus 48-51 18050914-7 2007 The storage stability of the co-immobilized GOD-CAT was also found to be higher than that of the free form at both 5 degrees C and 25 degrees C. The increased GOD activity and reusability resulting from the co-immobilization process may have been due to CAT protecting GOD from inactivation by H2O2 and supplying additional O2 to the reaction system. Hydrogen Peroxide 294-298 catalase Bos taurus 254-257 17183702-8 2006 An Escherichia coli mutant defective in the KatG catalase/peroxidase is sensitive to tellurite, and expression of the S. epidermidis catalase gene in a heterologous E. coli host confers increased resistance to tellurite as well as to hydrogen peroxide in vivo, arguing that S. epidermidis catalase provides a physiological line of defense against both of these strong oxidizing agents. Hydrogen Peroxide 234-251 catalase Bos taurus 49-57 17123644-3 2007 Here, we investigated the role of catalase, an enzyme responsible for H(2)O(2) detoxification. Hydrogen Peroxide 70-78 catalase Bos taurus 34-42 17385339-3 2007 The Vmax values for free and immobilized CAT were found to be 1.7 x 10(5) and 2.0 x 10(4) micromol H2O2 min(-1) mg protein(-1), respectively, whereas KM values were 33.3 mM and 1722.0 mM respectively. Hydrogen Peroxide 99-103 catalase Bos taurus 41-44 17067684-11 2007 The ability of these assays to discriminate between intra- and extracellular ROS and to specifically detect distinct ROS was evaluated using superoxide dismutase and catalase, which scavenge extracellular superoxide and hydrogen peroxide, respectively. Hydrogen Peroxide 220-237 catalase Bos taurus 166-174 17183702-8 2006 An Escherichia coli mutant defective in the KatG catalase/peroxidase is sensitive to tellurite, and expression of the S. epidermidis catalase gene in a heterologous E. coli host confers increased resistance to tellurite as well as to hydrogen peroxide in vivo, arguing that S. epidermidis catalase provides a physiological line of defense against both of these strong oxidizing agents. Hydrogen Peroxide 234-251 catalase Bos taurus 133-141 17183702-8 2006 An Escherichia coli mutant defective in the KatG catalase/peroxidase is sensitive to tellurite, and expression of the S. epidermidis catalase gene in a heterologous E. coli host confers increased resistance to tellurite as well as to hydrogen peroxide in vivo, arguing that S. epidermidis catalase provides a physiological line of defense against both of these strong oxidizing agents. Hydrogen Peroxide 234-251 catalase Bos taurus 133-141 16298761-0 2006 Non-oxygen-forming pathways of hydrogen peroxide degradation by bovine liver catalase at low hydrogen peroxide fluxes. Hydrogen Peroxide 31-48 catalase Bos taurus 77-85 16386389-13 2006 The addition of catalase to mixed cultures partially abolished the inhibition, an effect that could be attributed to the combined action of H2O2 and other antagonistic metabolites. Hydrogen Peroxide 140-144 catalase Bos taurus 16-24 16298761-0 2006 Non-oxygen-forming pathways of hydrogen peroxide degradation by bovine liver catalase at low hydrogen peroxide fluxes. Hydrogen Peroxide 93-110 catalase Bos taurus 77-85 15971617-7 2004 Catalase production by T. aurantiacus WSH 03-01 was further improved by optimizing the initial pH, volume of medium in flasks as well as the concentration of external H2O2. Hydrogen Peroxide 167-171 catalase Bos taurus 0-8 15233473-5 2004 Catalase (100 microg/ml) significantly reduced the sperm capacitation to 16-18% when added with H2O2, or alone in the capacitation medium. Hydrogen Peroxide 96-100 catalase Bos taurus 0-8 11110034-1 2000 In the present study, we examined the effect of inhibition of catalase with 3-aminotriazole (3-AT) on hydrogen peroxide (H2O2)-induced enhancement of sympathetic neurotransmission in bovine irides and on the inhibitory effect of this oxidant on norepinephrine (NE) release from human irides, in vitro. Hydrogen Peroxide 102-119 catalase Bos taurus 62-70 12788228-8 2003 Antioxidants, such as catalase (CAT) and dimethylthiourea (DMTU), which were able to block the H(2)O(2)-induced changes, had no effect on the MQ-induced permeability and GSH changes, suggesting that H(2)O(2) was not involved in MQ-induced effects. Hydrogen Peroxide 95-103 catalase Bos taurus 22-30 12788228-8 2003 Antioxidants, such as catalase (CAT) and dimethylthiourea (DMTU), which were able to block the H(2)O(2)-induced changes, had no effect on the MQ-induced permeability and GSH changes, suggesting that H(2)O(2) was not involved in MQ-induced effects. Hydrogen Peroxide 95-103 catalase Bos taurus 32-35 12760471-9 2003 Catalase (10 U/mL) increased the percentage of viable cells and reduced LDH release in H2O2-treated BAE and BBME, suggesting that DS likely acts by a different mechanism and does not neutralize H2O2. Hydrogen Peroxide 87-91 catalase Bos taurus 0-8 12438404-3 2002 Inhibition was neutralized by bovine catalase, suggesting that H(2)O(2) is the primary mediator of inhibition. Hydrogen Peroxide 63-71 catalase Bos taurus 37-45 11949860-6 2002 Melatonin has been reported to scavenge hydroxyl radical and peroxynitrite, whereas catalase and superoxide dismutase scavenge hydrogen peroxide and superoxide, respectively. Hydrogen Peroxide 127-144 catalase Bos taurus 84-92 11068675-5 2000 In a medium containing 0.1 mM hydrogen peroxide, its toxic effect on L. reuteri JCM 1112 was abolished by catalase or B. subtilis (natto). Hydrogen Peroxide 30-47 catalase Bos taurus 106-114 12041904-10 2002 Addition of only 5 U/ml of bovine liver catalase or oviductal fluid catalase (OFC) were sufficient to overcome the loss of sperm motility caused by 100 microM H2O2 in both EYTG and TALP. Hydrogen Peroxide 159-163 catalase Bos taurus 40-48 12041904-10 2002 Addition of only 5 U/ml of bovine liver catalase or oviductal fluid catalase (OFC) were sufficient to overcome the loss of sperm motility caused by 100 microM H2O2 in both EYTG and TALP. Hydrogen Peroxide 159-163 catalase Bos taurus 68-76 12041904-13 2002 Moreover, EDTA, pyruvate and catalase prevented sperm ATP loss in presence of 100 mM of H2O2 in EYTG. Hydrogen Peroxide 88-92 catalase Bos taurus 29-37 11388909-5 2001 Analyses of the enzymatic activities of GPx and catalase support the RNA data, indicating that H(2)O(2) produced due to the lack of GPx is a potent inducer of luteal cell apoptosis. Hydrogen Peroxide 95-103 catalase Bos taurus 48-56 11071366-6 2000 In support of an intermediary role of superoxide ions or H2O2 in the action of glutathione/Fe2+ system, superoxide dismutase and catalase expressed a substantial protection against the inactivation by the glutathione/Fe2+ system. Hydrogen Peroxide 57-61 catalase Bos taurus 129-137 11110034-1 2000 In the present study, we examined the effect of inhibition of catalase with 3-aminotriazole (3-AT) on hydrogen peroxide (H2O2)-induced enhancement of sympathetic neurotransmission in bovine irides and on the inhibitory effect of this oxidant on norepinephrine (NE) release from human irides, in vitro. Hydrogen Peroxide 121-125 catalase Bos taurus 62-70 9849623-2 1998 The rate of consumption of H2O2 in chloroform catalyzed by the lyophilized catalase with 3 was enhanced more than 10 times that by catalase without 3. Hydrogen Peroxide 27-31 catalase Bos taurus 75-83 10209276-0 1999 Influence of different types of effectors on the kinetic parameters of suicide inactivation of catalase by hydrogen peroxide. Hydrogen Peroxide 107-124 catalase Bos taurus 95-103 10385036-2 1999 Evidence exists for the participation of hydrogen peroxide-dependent regulation of prostaglandin production and soluble guanylate cyclase activity, resulting from the metabolism of peroxide by cyclooxygenase and catalase, respectively, in P(O2)-elicited signalling mechanisms that regulate vascular force generation. Hydrogen Peroxide 41-58 catalase Bos taurus 212-220 9849623-2 1998 The rate of consumption of H2O2 in chloroform catalyzed by the lyophilized catalase with 3 was enhanced more than 10 times that by catalase without 3. Hydrogen Peroxide 27-31 catalase Bos taurus 131-139 9275276-4 1997 Anamorphoses of complete kinetic curves as a function of 1/ln([H2O2]0/[H2O2]t) versus 1/t were used for calculation of the effective rate constants of catalase inactivation during the reaction (k(in), sec-1) and the rate constants of interaction of catalase complex I with the second molecule of H2O2 (k2, M-1.sec-1). Hydrogen Peroxide 63-67 catalase Bos taurus 151-159 9592089-1 1998 Catalase is an antioxidant enzyme that has been shown to inhibit apoptotic or necrotic neuronal death induced by hydrogen peroxide. Hydrogen Peroxide 113-130 catalase Bos taurus 0-8 9537289-12 1998 Presence of catalase (0.01 mg/ml) in the amino acid-supplemented Sp-Talp for 6 hours kept sperm motility and velocity at control levels, suggesting that the toxic effect of amino acids acts on sperm by excess hydrogen peroxide production. Hydrogen Peroxide 209-226 catalase Bos taurus 12-20 9541866-0 1997 The effects of temperature and pH on the kinetics of reactions between catalase and its suicide substrate hydrogen peroxide. Hydrogen Peroxide 106-123 catalase Bos taurus 71-79 9541866-1 1997 Variation of initial (intact) activity (ai), inactivation rate constant (ki) and the partition ratio (r) of bovine liver catalase in the reaction with its suicide substrate, hydrogen peroxide, were determined in workable ranges of temperature (17-42 degrees C) or pH (5-10.5), using the data of progress curves. Hydrogen Peroxide 174-191 catalase Bos taurus 121-129 9541866-5 1997 In pH studies, decreasing of pH from 7.0 to 5.0 led to reduction of ai whereas the ki value was not effected significantly, possibly due to the parallel changes in affinities to free catalase and compound I for H2O2. Hydrogen Peroxide 211-215 catalase Bos taurus 183-191 9803413-11 1998 In the presence of a H2O2-generating system, catalase activity of rAsCAT was inhibited by 3-aminotriazole, phenolic compounds, and drugs. Hydrogen Peroxide 21-25 catalase Bos taurus 45-53 9620079-4 1998 Catalase activity was measured by H2O2 decomposition, usually at 100 microM and 10 mM H2O2, and in some cases by O2 generation. Hydrogen Peroxide 34-38 catalase Bos taurus 0-8 9620079-4 1998 Catalase activity was measured by H2O2 decomposition, usually at 100 microM and 10 mM H2O2, and in some cases by O2 generation. Hydrogen Peroxide 86-90 catalase Bos taurus 0-8 9620079-14 1998 Catalase may be the macromolecular component responsible for aqueous H2O2 decay, as evidenced by H2O2 degradation, inhibition by boiling or 3-aminotriazole, and the approximate correspondence between oxygen generation and H2O2 degradation. Hydrogen Peroxide 69-73 catalase Bos taurus 0-8 9620079-14 1998 Catalase may be the macromolecular component responsible for aqueous H2O2 decay, as evidenced by H2O2 degradation, inhibition by boiling or 3-aminotriazole, and the approximate correspondence between oxygen generation and H2O2 degradation. Hydrogen Peroxide 97-101 catalase Bos taurus 0-8 9620079-14 1998 Catalase may be the macromolecular component responsible for aqueous H2O2 decay, as evidenced by H2O2 degradation, inhibition by boiling or 3-aminotriazole, and the approximate correspondence between oxygen generation and H2O2 degradation. Hydrogen Peroxide 97-101 catalase Bos taurus 0-8 9510962-3 1998 Catalase activates the decomposition of H2O2 into water and oxygen, thus removing an initiator of free radical chain reactions leading to lipid peroxidation. Hydrogen Peroxide 40-44 catalase Bos taurus 0-8 9275276-4 1997 Anamorphoses of complete kinetic curves as a function of 1/ln([H2O2]0/[H2O2]t) versus 1/t were used for calculation of the effective rate constants of catalase inactivation during the reaction (k(in), sec-1) and the rate constants of interaction of catalase complex I with the second molecule of H2O2 (k2, M-1.sec-1). Hydrogen Peroxide 71-75 catalase Bos taurus 151-159 9275276-4 1997 Anamorphoses of complete kinetic curves as a function of 1/ln([H2O2]0/[H2O2]t) versus 1/t were used for calculation of the effective rate constants of catalase inactivation during the reaction (k(in), sec-1) and the rate constants of interaction of catalase complex I with the second molecule of H2O2 (k2, M-1.sec-1). Hydrogen Peroxide 71-75 catalase Bos taurus 151-159 9275276-7 1997 Operational stability of yeast catalase is 3.5-fold higher than the stability of bovine catalase and much higher during cyclic decomposition of 50 mM H2O2. Hydrogen Peroxide 150-154 catalase Bos taurus 31-39 9868112-2 1997 It was found that, when compared with unpretreated cells, H2O2-induced the release of lactate dehydrogenase and the production of thiobarbituric acid reactive substances were decreased, at the meantime the cellular activites of catalase and superoxide dismutase were maintained in DFX (2 mmol.L-1) pretreated BPAECs challenged by 1 mmol.L-1 H2O2. Hydrogen Peroxide 58-62 catalase Bos taurus 228-236 9868112-2 1997 It was found that, when compared with unpretreated cells, H2O2-induced the release of lactate dehydrogenase and the production of thiobarbituric acid reactive substances were decreased, at the meantime the cellular activites of catalase and superoxide dismutase were maintained in DFX (2 mmol.L-1) pretreated BPAECs challenged by 1 mmol.L-1 H2O2. Hydrogen Peroxide 341-345 catalase Bos taurus 228-236 8980644-1 1996 A study of the azide reaction with bovine liver catalase in presence of hydrogen peroxide has been performed, using conventional UV-visible spectrometry and activity measurements. Hydrogen Peroxide 72-89 catalase Bos taurus 48-56 8980644-5 1996 Catalase is irreversibly inactivated by prolonged exposure to high levels of H2O2 and azide. Hydrogen Peroxide 77-81 catalase Bos taurus 0-8 8945907-8 1996 Thus exposure of pulmonary arteries to increased physiological levels of NO may promote altered vasoactive responses involving H2O2 as a result of the inhibition of catalase. Hydrogen Peroxide 127-131 catalase Bos taurus 165-173 8945907-7 1996 The exposure of pulmonary arteries to NO also resulted in the detection of H2O2 release (by catalase-inhibitable luminol/ peroxidase-chemiluminescence). Hydrogen Peroxide 75-79 catalase Bos taurus 92-100 8605985-4 1996 Catalase is a ubiquitous enzyme that is an important scavenger of hydrogen peroxide in vivo. Hydrogen Peroxide 66-83 catalase Bos taurus 0-8 8695649-0 1996 Reversible inhibition and irreversible inactivation of catalase in presence of hydrogen peroxide. Hydrogen Peroxide 79-96 catalase Bos taurus 55-63 8695649-1 1996 Spectroscopic and kinetic investigations have been carried out on catalase from bovine liver and from Aspergillus niger to address the mechanism of activity loss at high hydrogen peroxide concentrations (0.01 to 2 M). Hydrogen Peroxide 170-187 catalase Bos taurus 66-74 8695649-3 1996 A comparison of reaction rates with catalase preparations containing different proportions of Compound III indicated that the formation of Compound III is responsible for the reversible inhibition of bovine liver catalase at high H2O2 concentrations. Hydrogen Peroxide 230-234 catalase Bos taurus 36-44 8695649-3 1996 A comparison of reaction rates with catalase preparations containing different proportions of Compound III indicated that the formation of Compound III is responsible for the reversible inhibition of bovine liver catalase at high H2O2 concentrations. Hydrogen Peroxide 230-234 catalase Bos taurus 213-221 8945907-1 1996 Our previous studies on the mechanism of relaxation of calf pulmonary arteries to H2O2 detected a role for increased formation of guanosine-3",5"-cyclic monophosphate as a result of a catalase-elicited activation of soluble guanylate cyclase. Hydrogen Peroxide 82-86 catalase Bos taurus 184-192 8945907-5 1996 This NO exposure caused a 63 and 70% inhibition of the metabolism by smooth muscle catalase of both endogenously produced and exogenous (100 microM) H2O2, respectively, as measured by the H2O2-dependent cooxidation of methanol to formaldehyde. Hydrogen Peroxide 149-153 catalase Bos taurus 83-91 8945907-5 1996 This NO exposure caused a 63 and 70% inhibition of the metabolism by smooth muscle catalase of both endogenously produced and exogenous (100 microM) H2O2, respectively, as measured by the H2O2-dependent cooxidation of methanol to formaldehyde. Hydrogen Peroxide 188-192 catalase Bos taurus 83-91 8945907-6 1996 A similar treatment of purified catalase with NO caused subsequent inhibition of its ability to metabolize H2O2, associated with changes in the spectra of catalase (increases in the absorbance at 535 and 570 nm) to a species that resembled compound II, an inactive form of catalase. Hydrogen Peroxide 107-111 catalase Bos taurus 32-40 8945907-6 1996 A similar treatment of purified catalase with NO caused subsequent inhibition of its ability to metabolize H2O2, associated with changes in the spectra of catalase (increases in the absorbance at 535 and 570 nm) to a species that resembled compound II, an inactive form of catalase. Hydrogen Peroxide 107-111 catalase Bos taurus 155-163 8945907-6 1996 A similar treatment of purified catalase with NO caused subsequent inhibition of its ability to metabolize H2O2, associated with changes in the spectra of catalase (increases in the absorbance at 535 and 570 nm) to a species that resembled compound II, an inactive form of catalase. Hydrogen Peroxide 107-111 catalase Bos taurus 155-163 8856848-2 1996 The bovine pulmonary artery endothelial cells (BPAECs) heat-shocked (42 degrees C for 2 h) prior to exposure to H2O2 (1 mmol/L for 45 min) showed significant decrease in H2O2-mediated increment of release of lactate dehydrogenase and production of thiobarbituric acid-reactive substances, and obvious alleviation in H2O2-induced decrease in activities of catalase and superoxide dismutase. Hydrogen Peroxide 112-116 catalase Bos taurus 355-363 8856848-2 1996 The bovine pulmonary artery endothelial cells (BPAECs) heat-shocked (42 degrees C for 2 h) prior to exposure to H2O2 (1 mmol/L for 45 min) showed significant decrease in H2O2-mediated increment of release of lactate dehydrogenase and production of thiobarbituric acid-reactive substances, and obvious alleviation in H2O2-induced decrease in activities of catalase and superoxide dismutase. Hydrogen Peroxide 170-174 catalase Bos taurus 355-363 8856848-2 1996 The bovine pulmonary artery endothelial cells (BPAECs) heat-shocked (42 degrees C for 2 h) prior to exposure to H2O2 (1 mmol/L for 45 min) showed significant decrease in H2O2-mediated increment of release of lactate dehydrogenase and production of thiobarbituric acid-reactive substances, and obvious alleviation in H2O2-induced decrease in activities of catalase and superoxide dismutase. Hydrogen Peroxide 170-174 catalase Bos taurus 355-363 8743587-8 1996 We concluded that selenium-deficient cells were more easily brought to apoptotic cell death by peroxides, but not by superoxide radicals, than selenium-supplemented ones and that CAT could compensate for the depletion of GPx to a certain degree by scavenging H2O2. Hydrogen Peroxide 259-263 catalase Bos taurus 179-182 8598569-1 1996 The effect of diesel exhaust particles (DEP) on the activity of catalase, an intracellular antioxidant, was investigated because H2O2 is a cytotoxic oxidant, and catalase released from alveolar cells is an important antioxidant in the epithelial lining fluid in the lung. Hydrogen Peroxide 129-133 catalase Bos taurus 64-72 7672008-7 1995 Catalase drastically protected against the cytotoxic effects of 6-hydroxydopamine and H2O2. Hydrogen Peroxide 86-90 catalase Bos taurus 0-8 8835942-0 1996 Determination of the kinetic parameters for the "suicide substrate" inactivation of bovine liver catalase by hydrogen peroxide. Hydrogen Peroxide 109-126 catalase Bos taurus 97-105 8835942-1 1996 The kinetics of the bovine liver catalase inactivation by its suicide substrate, H2O2 was investigated in sodium phosphate buffer, 50 mM pH 7.0, at 27 degrees C. By combination of the rate equations of two concurrent reactions, decomposition of H2O2 by catalase and suicide inactivation of catalase by H2O2, simple, semiempirical kinetic equations were defined and used for the determination of the inactivation rate constant and the partition ratio which were found to be 6.86 +/- 0.19 M-1 min-1 and 1.82 x 10(7) +/- 5.0 x 10(5), respectively. Hydrogen Peroxide 81-85 catalase Bos taurus 33-41 8835942-1 1996 The kinetics of the bovine liver catalase inactivation by its suicide substrate, H2O2 was investigated in sodium phosphate buffer, 50 mM pH 7.0, at 27 degrees C. By combination of the rate equations of two concurrent reactions, decomposition of H2O2 by catalase and suicide inactivation of catalase by H2O2, simple, semiempirical kinetic equations were defined and used for the determination of the inactivation rate constant and the partition ratio which were found to be 6.86 +/- 0.19 M-1 min-1 and 1.82 x 10(7) +/- 5.0 x 10(5), respectively. Hydrogen Peroxide 81-85 catalase Bos taurus 253-261 8835942-1 1996 The kinetics of the bovine liver catalase inactivation by its suicide substrate, H2O2 was investigated in sodium phosphate buffer, 50 mM pH 7.0, at 27 degrees C. By combination of the rate equations of two concurrent reactions, decomposition of H2O2 by catalase and suicide inactivation of catalase by H2O2, simple, semiempirical kinetic equations were defined and used for the determination of the inactivation rate constant and the partition ratio which were found to be 6.86 +/- 0.19 M-1 min-1 and 1.82 x 10(7) +/- 5.0 x 10(5), respectively. Hydrogen Peroxide 81-85 catalase Bos taurus 253-261 8835942-1 1996 The kinetics of the bovine liver catalase inactivation by its suicide substrate, H2O2 was investigated in sodium phosphate buffer, 50 mM pH 7.0, at 27 degrees C. By combination of the rate equations of two concurrent reactions, decomposition of H2O2 by catalase and suicide inactivation of catalase by H2O2, simple, semiempirical kinetic equations were defined and used for the determination of the inactivation rate constant and the partition ratio which were found to be 6.86 +/- 0.19 M-1 min-1 and 1.82 x 10(7) +/- 5.0 x 10(5), respectively. Hydrogen Peroxide 245-249 catalase Bos taurus 33-41 8835942-1 1996 The kinetics of the bovine liver catalase inactivation by its suicide substrate, H2O2 was investigated in sodium phosphate buffer, 50 mM pH 7.0, at 27 degrees C. By combination of the rate equations of two concurrent reactions, decomposition of H2O2 by catalase and suicide inactivation of catalase by H2O2, simple, semiempirical kinetic equations were defined and used for the determination of the inactivation rate constant and the partition ratio which were found to be 6.86 +/- 0.19 M-1 min-1 and 1.82 x 10(7) +/- 5.0 x 10(5), respectively. Hydrogen Peroxide 245-249 catalase Bos taurus 253-261 8835942-1 1996 The kinetics of the bovine liver catalase inactivation by its suicide substrate, H2O2 was investigated in sodium phosphate buffer, 50 mM pH 7.0, at 27 degrees C. By combination of the rate equations of two concurrent reactions, decomposition of H2O2 by catalase and suicide inactivation of catalase by H2O2, simple, semiempirical kinetic equations were defined and used for the determination of the inactivation rate constant and the partition ratio which were found to be 6.86 +/- 0.19 M-1 min-1 and 1.82 x 10(7) +/- 5.0 x 10(5), respectively. Hydrogen Peroxide 245-249 catalase Bos taurus 253-261 8835942-1 1996 The kinetics of the bovine liver catalase inactivation by its suicide substrate, H2O2 was investigated in sodium phosphate buffer, 50 mM pH 7.0, at 27 degrees C. By combination of the rate equations of two concurrent reactions, decomposition of H2O2 by catalase and suicide inactivation of catalase by H2O2, simple, semiempirical kinetic equations were defined and used for the determination of the inactivation rate constant and the partition ratio which were found to be 6.86 +/- 0.19 M-1 min-1 and 1.82 x 10(7) +/- 5.0 x 10(5), respectively. Hydrogen Peroxide 245-249 catalase Bos taurus 33-41 8835942-1 1996 The kinetics of the bovine liver catalase inactivation by its suicide substrate, H2O2 was investigated in sodium phosphate buffer, 50 mM pH 7.0, at 27 degrees C. By combination of the rate equations of two concurrent reactions, decomposition of H2O2 by catalase and suicide inactivation of catalase by H2O2, simple, semiempirical kinetic equations were defined and used for the determination of the inactivation rate constant and the partition ratio which were found to be 6.86 +/- 0.19 M-1 min-1 and 1.82 x 10(7) +/- 5.0 x 10(5), respectively. Hydrogen Peroxide 245-249 catalase Bos taurus 253-261 8835942-1 1996 The kinetics of the bovine liver catalase inactivation by its suicide substrate, H2O2 was investigated in sodium phosphate buffer, 50 mM pH 7.0, at 27 degrees C. By combination of the rate equations of two concurrent reactions, decomposition of H2O2 by catalase and suicide inactivation of catalase by H2O2, simple, semiempirical kinetic equations were defined and used for the determination of the inactivation rate constant and the partition ratio which were found to be 6.86 +/- 0.19 M-1 min-1 and 1.82 x 10(7) +/- 5.0 x 10(5), respectively. Hydrogen Peroxide 245-249 catalase Bos taurus 253-261 7793971-0 1995 Inactivation of an animal and a fungal catalase by hydrogen peroxide. Hydrogen Peroxide 51-68 catalase Bos taurus 39-47 7793971-12 1995 It appears unlikely that compound II is an intermediate in the hydrogen peroxide-mediated inactivation reaction of either catalase under catalatic assay conditions. Hydrogen Peroxide 63-80 catalase Bos taurus 122-130 7757201-0 1995 Reactions of bovine liver catalase with superoxide radicals and hydrogen peroxide. Hydrogen Peroxide 64-81 catalase Bos taurus 26-34 7757201-1 1995 The oxidized intermediates generated upon exposure of bovine liver catalase to hydrogen peroxide (H2O2) and superoxide radical (O2-) fluxes were examined with UV-visible spectrophotometry. Hydrogen Peroxide 98-102 catalase Bos taurus 67-75 7757201-3 1995 Serial overlay of absorption spectra in the Soret (350-450 nm) and visible (450-700 nm) regions showed that three oxidized intermediates, namely Compounds I, II and III, can be observed upon exposure of catalase to enzymatically generated H2O2 and O2-. Hydrogen Peroxide 239-243 catalase Bos taurus 203-211 7757201-1 1995 The oxidized intermediates generated upon exposure of bovine liver catalase to hydrogen peroxide (H2O2) and superoxide radical (O2-) fluxes were examined with UV-visible spectrophotometry. Hydrogen Peroxide 79-96 catalase Bos taurus 67-75 7757201-4 1995 Compound I is formed during the reaction of native enzyme with H2O2 and disappears in two ways: (i) via the catalytic reaction with H2O2 to restore native catalase and (ii) via the reaction with O2- to form Compound II. Hydrogen Peroxide 63-67 catalase Bos taurus 155-163 1748479-4 1991 The supplementation of the culture media with catalase, which degrades hydrogen peroxide, either alone or in combination with indomethacin, also did not result in restoration of proliferation. Hydrogen Peroxide 71-88 catalase Bos taurus 46-54 8460674-6 1993 In addition, H2O2 induced an increase in antioxidative enzyme activities in the VEC, including superoxide dismutase, catalase, and glutathione peroxidase. Hydrogen Peroxide 13-17 catalase Bos taurus 117-125 1568306-11 1992 Treatment with catalase (100-1,000 units/ml) inhibited the reoxygenation-induced increase in permeability at the highest catalase concentration (1,000 units/ml), suggesting a critical role of hydrogen peroxide in mediating the response. Hydrogen Peroxide 192-209 catalase Bos taurus 15-23 18609542-1 1993 The quasi-steady behavior of a continuous flow reactor in which hydrogen peroxide is decomposed by immobilized catalase is investigated. Hydrogen Peroxide 64-81 catalase Bos taurus 111-119 1567224-4 1992 We determined a basal intracellular H2O2 concentration of 32.8 +/- 10.7 pM in cultured bovine aortic endothelial cells by kinetic analysis of aminotriazole-mediated inactivation of endogenous catalase. Hydrogen Peroxide 36-40 catalase Bos taurus 192-200 1646767-0 1991 Elimination of hydrogen peroxide by Haemophilus somnus, a catalase-negative pathogen of cattle. Hydrogen Peroxide 15-32 catalase Bos taurus 58-66 1646767-5 1991 We have presented evidence that four separate strains of H. somnus, despite being catalase negative by conventional criteria, removed H2O2 from solution. Hydrogen Peroxide 134-138 catalase Bos taurus 82-90 2575561-7 1989 These observations indicate that autoxidation of ascorbic acid or thiols present with the guanylate cyclase preparation leads to generation of H2O2, and its metabolism by bovine liver catalase mediates the concomitant activation of guanylate cyclase. Hydrogen Peroxide 143-147 catalase Bos taurus 184-192 2556049-3 1989 Catalase, but not mannitol or superoxide dismutase, prevented endothelial cell injury induced by HX/XO, indicating that H2O2 was the mediator of the cytotoxicity. Hydrogen Peroxide 120-124 catalase Bos taurus 0-8 18597274-0 1990 Deactivation of catalase by hydrogen peroxide. Hydrogen Peroxide 28-45 catalase Bos taurus 16-24 1970924-1 1990 We have recently suggested that relaxation of isolated precontracted intrapulmonary arteries from calves to H2O2 or O2 may involve the activation of guanylate cyclase by peroxide metabolism via catalase. Hydrogen Peroxide 108-112 catalase Bos taurus 194-202 1690958-2 1990 Spontaneous oxidation of Na2S2O4 and the enzymatic reduction of NaBO3 or H2O2 by bovine liver catalase trapped in hydrated micelles of dioctylsulfosuccinate (AOT)/toluene were used as model systems. Hydrogen Peroxide 73-77 catalase Bos taurus 94-102 34818079-9 2022 However, the addition of catalase (7,000 U/mL) to rapidly decompose H2O2 limited the loss in TER. Hydrogen Peroxide 68-72 catalase Bos taurus 25-33 2575561-0 1989 Ascorbate activates soluble guanylate cyclase via H2O2-metabolism by catalase. Hydrogen Peroxide 50-54 catalase Bos taurus 69-77 3597427-1 1987 We find ethanenitronate (formula; see text) to be a H2O2- (and peracetic acid-) dependent suicide substrate for bovine liver catalase (E) which converts E to Em, a modified form of the enzyme. Hydrogen Peroxide 52-56 catalase Bos taurus 125-133 2562975-4 1989 The rate constant of formation of Compound I due to the reaction of catalase with hydrogen peroxide has been estimated to be 2.0 x 10(7) dm3mol-1s-1. Hydrogen Peroxide 82-99 catalase Bos taurus 68-76 2881544-0 1987 Hydrogen peroxide elicits activation of bovine pulmonary arterial soluble guanylate cyclase by a mechanism associated with its metabolism by catalase. Hydrogen Peroxide 0-17 catalase Bos taurus 141-149 2881544-1 1987 Guanylate cyclase activity in the soluble extract of bovine pulmonary arteries is activated by hydrogen peroxide generated by glucose oxidase only in the presence of catalase. Hydrogen Peroxide 95-112 catalase Bos taurus 166-174 3823631-3 1987 The levels of two enzymes, superoxide dismutase and catalase, involved in the removal of superoxide anion and hydrogen peroxide, were compared in Hereford cattle predisposed to ocular carcinoma and a resistant breed, Droughtmaster cattle. Hydrogen Peroxide 110-127 catalase Bos taurus 52-60 3783731-7 1986 Since both ascorbate and catalase but not superoxide dismutase inhibited relaxation, it appears that hydrogen peroxide is involved. Hydrogen Peroxide 101-118 catalase Bos taurus 25-33 6323471-4 1984 The formation of Compound I is due to the reaction of ferric catalase with hydrogen peroxide, which is generated by the disproportionation of the superoxide anion (O-2). Hydrogen Peroxide 75-92 catalase Bos taurus 61-69 3761960-1 1986 Catalase may provide protection against photochemical action of superoxide radicals and hydrogen peroxide. Hydrogen Peroxide 88-105 catalase Bos taurus 0-8 3840689-2 1985 Through the use of catalase, superoxide dismutase and the specific iron chelator diethylenetriaminepentaacetic acid, the active species responsible for inhibition was shown to be hydrogen peroxide. Hydrogen Peroxide 179-196 catalase Bos taurus 19-27 3985946-6 1985 Diaminobenzidine protects catalase against the irreversible inactivation imposed by 3-amino-1,2,4-triazole plus H2O2. Hydrogen Peroxide 112-116 catalase Bos taurus 26-34 3004685-4 1985 There appeared to be a relationship between high endogenous catalase levels and the high H2O2 evolution and KCN insensitivity of B. coagulans respiration. Hydrogen Peroxide 89-93 catalase Bos taurus 60-68 4044161-8 1985 At physiologic H2O2 concentrations, catalase may have similar levels of activity to glutathione peroxidase. Hydrogen Peroxide 15-19 catalase Bos taurus 36-44 6189332-5 1983 Hydrogen peroxide plays an important role in this reaction: the rates of formation of both dopa and 6-OH-dopa were increased by addition of hydrogen peroxide but diminished by addition of catalase. Hydrogen Peroxide 0-17 catalase Bos taurus 188-196 6372321-4 1983 The mechanism of microbial antagonism was due to production and release of hydrogen peroxide under aerobic atmospheric conditions, which was neutralized through incorporation of bovine liver catalase into the solid assay medium. Hydrogen Peroxide 75-92 catalase Bos taurus 191-199 6830896-0 1983 [Influence of magnetic field on hydrogen peroxide decomposition by catalase]. Hydrogen Peroxide 32-49 catalase Bos taurus 67-76 24276825-5 1981 Since the decarboxylation of both substrates was greatly in creased by the catalase inhibitor, 3-amino-1,2,4-triazole, and abolished by bovine liver catalase, it was attributed to the nonenzymic attack of H2O2, generated in glycollate oxidation, upon glyoxylate and hydroxypyruvate respectively. Hydrogen Peroxide 205-209 catalase Bos taurus 75-83 24276825-5 1981 Since the decarboxylation of both substrates was greatly in creased by the catalase inhibitor, 3-amino-1,2,4-triazole, and abolished by bovine liver catalase, it was attributed to the nonenzymic attack of H2O2, generated in glycollate oxidation, upon glyoxylate and hydroxypyruvate respectively. Hydrogen Peroxide 205-209 catalase Bos taurus 149-157 940547-4 1976 When solutions of bovine liver catalase were re-incubated up to 24 hr under near-UV with preirradiated tryptophan and dialyzed, most of the ability of the enzyme to decompose H2O2 was lost. Hydrogen Peroxide 175-179 catalase Bos taurus 31-39 7407339-2 1980 The catalase-H2O2 system proved to be suitable during the growth at low cell densities equivalent to 2 g dry weight/liter. Hydrogen Peroxide 13-17 catalase Bos taurus 4-12 7407339-5 1980 The impairment of growth observed during the oxygen supply by the catalase-H2O2 system was traced back to the formation of gradually increasing steady-state concentrations of H2O2 in the medium. Hydrogen Peroxide 75-79 catalase Bos taurus 66-74 7407339-5 1980 The impairment of growth observed during the oxygen supply by the catalase-H2O2 system was traced back to the formation of gradually increasing steady-state concentrations of H2O2 in the medium. Hydrogen Peroxide 175-179 catalase Bos taurus 66-74 7407340-0 1980 Efficiency of bovine liver catalase as a catalyst to cleave H2O2 added continually to buffer solutions. Hydrogen Peroxide 60-64 catalase Bos taurus 27-35 7407340-3 1980 At a constant catalase concentration both the level and the duration of the steady state are dependent on the flow rate of H2O2. Hydrogen Peroxide 123-127 catalase Bos taurus 14-22 7407340-5 1980 At higher flow rates of H2O2, no steady state could be maintained, even when catalase was present in high excess. Hydrogen Peroxide 24-28 catalase Bos taurus 77-85 7407340-6 1980 The incomplete cleavage of H2O2 by catalase under these conditions is due to the low affinity of catalase toward H2O2 (high K m value, apparent K m = 0.1M H2O2) and to the rapid inactivation of the enzyme during the continuous addition of H2O2. Hydrogen Peroxide 27-31 catalase Bos taurus 35-43 7407340-6 1980 The incomplete cleavage of H2O2 by catalase under these conditions is due to the low affinity of catalase toward H2O2 (high K m value, apparent K m = 0.1M H2O2) and to the rapid inactivation of the enzyme during the continuous addition of H2O2. Hydrogen Peroxide 27-31 catalase Bos taurus 97-105 7407340-6 1980 The incomplete cleavage of H2O2 by catalase under these conditions is due to the low affinity of catalase toward H2O2 (high K m value, apparent K m = 0.1M H2O2) and to the rapid inactivation of the enzyme during the continuous addition of H2O2. Hydrogen Peroxide 113-117 catalase Bos taurus 35-43 7407340-6 1980 The incomplete cleavage of H2O2 by catalase under these conditions is due to the low affinity of catalase toward H2O2 (high K m value, apparent K m = 0.1M H2O2) and to the rapid inactivation of the enzyme during the continuous addition of H2O2. Hydrogen Peroxide 113-117 catalase Bos taurus 97-105 7407340-6 1980 The incomplete cleavage of H2O2 by catalase under these conditions is due to the low affinity of catalase toward H2O2 (high K m value, apparent K m = 0.1M H2O2) and to the rapid inactivation of the enzyme during the continuous addition of H2O2. Hydrogen Peroxide 113-117 catalase Bos taurus 35-43 7407340-6 1980 The incomplete cleavage of H2O2 by catalase under these conditions is due to the low affinity of catalase toward H2O2 (high K m value, apparent K m = 0.1M H2O2) and to the rapid inactivation of the enzyme during the continuous addition of H2O2. Hydrogen Peroxide 113-117 catalase Bos taurus 97-105 7407340-6 1980 The incomplete cleavage of H2O2 by catalase under these conditions is due to the low affinity of catalase toward H2O2 (high K m value, apparent K m = 0.1M H2O2) and to the rapid inactivation of the enzyme during the continuous addition of H2O2. Hydrogen Peroxide 113-117 catalase Bos taurus 35-43 7407340-6 1980 The incomplete cleavage of H2O2 by catalase under these conditions is due to the low affinity of catalase toward H2O2 (high K m value, apparent K m = 0.1M H2O2) and to the rapid inactivation of the enzyme during the continuous addition of H2O2. Hydrogen Peroxide 113-117 catalase Bos taurus 97-105 13587914-3 1958 The results of experiments in which hydrogen peroxide, catalase, or sodium azide were used singly or in combination suggest that the inhibition produced by the ascorbic acid oxidizing system is due, to a considerable extent, to the production of hydrogen peroxide. Hydrogen Peroxide 246-263 catalase Bos taurus 55-63