PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 7791219-1 1995 A catalase from a peroxide resistant mutant of Proteus mirabilis binds NADPH tightly. Peroxides 18-26 catalase Homo sapiens 2-10 9270070-4 1997 The use of specific chelators and catalase demonstrated that the reduction of Cu2+ to Cu1+ and the formation of a peroxide plays an important role in the activation of dopamine and 6-hydroxydopamine to form adducts and oxidative base damage. Peroxides 114-122 catalase Homo sapiens 34-42 8613912-5 1996 Addition of enzymes that metabolize peroxide (catalase or superoxide dismutase [SOD]) also reduced fluorescence by nearly 50%. Peroxides 36-44 catalase Homo sapiens 46-54 8552207-8 1995 It can be inferred that the accumulation of peroxides in the non-neoplastic colonic mucosa induced higher activities of CAT and GPx. Peroxides 44-53 catalase Homo sapiens 120-123 7906937-4 1994 When catalase, which degrades hydrogen peroxide produced by leukocytes, was added to this system, the peroxide level in endothelial cells decreased significantly. Peroxides 39-47 catalase Homo sapiens 5-13 8086159-5 1994 Therefore NADPH bound to Catalase is not essential to catalyze peroxidation processes or H2O2 dismutation, but it is essential to prevent the enzyme denaturation and to catalyze dismutation of peroxides other than H2O2. Peroxides 193-202 catalase Homo sapiens 25-33 1450598-1 1992 Superoxide dismutase, glutathione peroxidase and catalase are the three main enzymatic systems of defense of the organism against free radicals and peroxides. Peroxides 148-157 catalase Homo sapiens 49-57 8375696-1 1993 A feature of catalase that has received scant attention in recent years and that may have physiological significance is the peroxide-dependent inactivation of the enzyme. Peroxides 124-132 catalase Homo sapiens 13-21 11537538-7 1991 We suggest that atmospheric H2O2 played the key role in inducing oxygenic photosynthesis because as peroxide increased in a local environment, organisms would not only be faced with a loss of reductant, but they would also be pressed to develop the biochemical apparatus (e.g., catalase) that would ultimately be needed to protect against the products of oxygenic photosynthesis. Peroxides 100-108 catalase Homo sapiens 278-286 1793562-3 1991 The effects of the enzymes demonstrate that superoxide is a precursor to the rate-determining intermediate and that both catalase and peroxide enhance a reaction that competes with the rate-limiting process. Peroxides 46-54 catalase Homo sapiens 121-129 3340731-10 1988 Catalase reduced the rate of oxygen consumption of WR-1065, indicating that peroxide is formed in this system. Peroxides 76-84 catalase Homo sapiens 0-8 2308398-0 1990 Glutathione peroxidase, superoxide dismutase, and catalase inactivation by peroxides and oxygen derived free radicals. Peroxides 75-84 catalase Homo sapiens 50-58 34475406-1 2021 Peroxisome, a special cytoplasmic organelle, possesses one or more kinds of oxidases for hydrogen peroxide (H2O2) production and catalase for H2O2 degradation, which serves as an intracellular H2O2 regulator to degrade toxic peroxides to water. Peroxides 225-234 catalase Homo sapiens 129-137 34503517-13 2021 Unraveling these factors allowed to increase the FDCA yields by using the most stable enzymes at their optimal pH for HMF oxidation, removing the peroxide with catalase, and avoiding FFCA accumulation by controlling substrate and/or enzyme concentration. Peroxides 146-154 catalase Homo sapiens 160-168 3340731-13 1988 Since this stimulation was prevented by the presence of catalase, it appeared to be due to the response of the cells to peroxide, formed as a result of WR-1065 autooxidation. Peroxides 120-128 catalase Homo sapiens 56-64 6476384-4 1984 This problem has been avoided by extracting tissues with trichloroacetic acid, and measuring peroxide against catalase-treated blanks by its reaction with the complex of titanium(IV) with 4-(2-pyridylazo) resorcinol. Peroxides 93-101 catalase Homo sapiens 110-118 2429588-3 1986 Heated and unheated preparations could be used to demonstrate the presence of comigrating bands of M and T. The application of the ferricyanide stain after the DAB stain of T-catalase resulted in marked intensification of the positive bands of T-catalase due to nonenzymatic, peroxide-independent reduction of the ferricyanide by the DAB product. Peroxides 276-284 catalase Homo sapiens 175-183 2943713-6 1986 The addition of catalase, another important enzyme involved in peroxide reduction, partially reverses the observed toxicity. Peroxides 63-71 catalase Homo sapiens 16-24 7061348-5 1982 Two enzymes that regulate peroxide concentrations, catalase and glutathione peroxidase, were also prominent in both of these fractions. Peroxides 26-34 catalase Homo sapiens 51-59 689707-2 1978 Addition of pure H2O2 and use of the enzyme catalase demonstrate that about 40% of the toxicity in irradiated medium is due to generated peroxide. Peroxides 137-145 catalase Homo sapiens 44-52 30812193-5 1979 In addition, recent findings have indicated that the increased sensitivity of stressed staphylococci is at least partially due to hydrogen peroxide toxicity: based on these findings direct plating and most-probable-number techniques containing catalase to degrade peroxide have been proposed. Peroxides 139-147 catalase Homo sapiens 244-252 7290082-0 1981 Conversion of catalase to the secondary catalase-peroxide complex (compound II) by alpha-methyldopa. Peroxides 49-57 catalase Homo sapiens 14-22 7290082-0 1981 Conversion of catalase to the secondary catalase-peroxide complex (compound II) by alpha-methyldopa. Peroxides 49-57 catalase Homo sapiens 40-48 13160022-0 1954 The action of peroxidases with enzymically generated peroxide in the presence of catalase. Peroxides 53-61 catalase Homo sapiens 81-89 5082500-0 1972 Contributions of catalase and glutathione peroxidase to red cell peroxide removal. Peroxides 65-73 catalase Homo sapiens 17-25 14240966-7 1964 Cultures grown without catalase exhibited an absorption peak characteristic of peroxides. Peroxides 79-88 catalase Homo sapiens 23-31 14479448-0 1962 The reduction of catalase by azide and peroxides. Peroxides 39-48 catalase Homo sapiens 17-25 13008462-0 1952 Magnetic properties of some peroxide compounds of myoglobin, peroxidase and catalase. Peroxides 28-36 catalase Homo sapiens 76-84 639259-3 1978 The peroxide is reacted with ethanol in the presence of catalase to form acetaldehyde and water, and the acetaldehyde is reduced by NADH in the presence of alcohol dehydrogenase to ethanol. Peroxides 4-12 catalase Homo sapiens 56-64 14170320-0 1964 THE FORMATION AND CATALYTIC ROLE OF CATALASE PEROXIDE COMPOUND II. Peroxides 45-53 catalase Homo sapiens 36-44 13609101-0 1958 [The role of the catalase-reduced cytochrome system in the transfer of peroxide oxygen]. Peroxides 71-79 catalase Homo sapiens 17-25 13165628-0 1954 Reactions of methaemoglobin and catalase with peroxides and hydrogen donors. Peroxides 46-55 catalase Homo sapiens 32-40 19872144-0 1925 THE KINETICS OF THE DECOMPOSITION OF PEROXIDE BY CATALASE. Peroxides 37-45 catalase Homo sapiens 49-57 19872144-1 1925 It has been shown that the experimental results obtained by Morgulis in a study of the decomposition of hydrogen peroxide by liver catalase at 20 degrees C. and in the presence of an excess of a relatively high concentration of peroxide are quantitatively accounted for by the following mechanisms. Peroxides 113-121 catalase Homo sapiens 131-139 19872144-4 1925 The rate of decomposition of the peroxide is proportional at any time to the concentration of catalase present. Peroxides 33-41 catalase Homo sapiens 94-102 19872144-7 1925 This inactivation is independent of the concentration of catalase and inversely proportional to the original concentration of peroxide up to 0.4 M. In very high concentrations of peroxide the inactivation rate increases. Peroxides 179-187 catalase Homo sapiens 57-65 26901461-7 2016 Catalase, an enzyme decomposing peroxide, was found to suppress DNA damage at a NQO1/catalase ratio found in healthy cells, but was clearly overcome at a higher NQO1/catalase ratio consistent with cancer cells. Peroxides 32-40 catalase Homo sapiens 0-8 28566709-5 2017 In this work, we show that the C-At "organometalloid" bond can be cleaved by oxidative dehalogenation induced by oxidants such as permanganates, peroxides or hydroxyl radicals. Peroxides 145-154 catalase Homo sapiens 31-35 31498349-7 2019 The current assigned to the electrode oxidation of HA to AA decreased with the addition of catalase, a scavenger of H2O2, meaning peroxide is involved in the mechanism. Peroxides 131-139 catalase Homo sapiens 92-100 26901461-7 2016 Catalase, an enzyme decomposing peroxide, was found to suppress DNA damage at a NQO1/catalase ratio found in healthy cells, but was clearly overcome at a higher NQO1/catalase ratio consistent with cancer cells. Peroxides 32-40 catalase Homo sapiens 85-93 26347290-7 2015 The conversion of both O2 and OH(-) to a peroxide species is exactly the reverse of a catalase-like reaction, which has a great potential as the most efficient O2 activation. Peroxides 41-49 catalase Homo sapiens 86-94 26678800-5 2016 Furthermore PEG-catalase inhibited the DCFH2 oxidation signal to a greater extent in the ATRA-treated cells (relative to controls) at 96h indicating that as the cells became more differentiated, steady-state levels of H2O2 increased in the absence of increases in peroxide-scavenging antioxidants (i.e., glutathione, glutathione peroxidase, and catalase). Peroxides 264-272 catalase Homo sapiens 16-24 25813998-8 2015 RESULTS: After catalase transduction, high glucose-induced peroxide production was significantly lowered in both human retinal cell lines. Peroxides 59-67 catalase Homo sapiens 15-23 20874678-9 2010 The paradigm that, inhibiting the overproduction of superoxides and peroxides would prevent cardiac dysfunction in diabetes has been difficult to verify using conventional antioxidants like vitamins E and C. That led to use of catalytic antioxidants such as SOD/CAT mimetics. Peroxides 54-63 catalase Homo sapiens 262-265 25879557-13 2015 Activity of catalase was significantly increased in psoriatic patients, reflecting a high concentration of peroxide radicals. Peroxides 107-115 catalase Homo sapiens 12-20 22326823-1 2012 This review describes the historical difficulties in devising a kinetically satisfactory mechanism for the classical catalase after its identification as a unique catalytic entity in 1902 and prior to the breakthrough 1947 analysis by Chance and co-workers which led to the identification of peroxide compounds I and II. Peroxides 292-300 catalase Homo sapiens 117-125 20070187-1 2010 Catalase, glutathione peroxidase1 (GPx1), and peroxiredoxin (Prx) II are the principal enzymes responsible for peroxide elimination in RBC. Peroxides 111-119 catalase Homo sapiens 0-8 20688754-5 2010 We overcame this obstacle by pretreatment of the reaction solution with the enzyme catalase, which consumed endogenous peroxides resulting in reduced background and increased sensitivity in our method. Peroxides 119-128 catalase Homo sapiens 83-91 18063869-2 2008 Erythrocyte catalase (CAT) and cellular glutathione peroxidase (c-GPx) are antioxidant enzymes that detoxify peroxides generated from dismutation of superoxide anion. Peroxides 109-118 catalase Homo sapiens 12-20 18814949-5 2008 After the validation, the isoconversional method was used for the investigation of the thermoinactivation of urease during urea hydrolysis in self buffered medium and the operational inactivation (destructive oxidation by excess peroxide) of catalase at high concentration of hydrogen peroxide. Peroxides 229-237 catalase Homo sapiens 242-250 18231625-6 2008 Also the protection against exogenous and endogenous peroxides in the erythrocytes of alcoholic women is considerably affected due to decreased (p<0.05) activity of catalase, glucose-6-phosphate dehydrogenase, protein-SH group and glutathione (GSH). Peroxides 53-62 catalase Homo sapiens 168-176 17955493-5 2008 Interestingly, an increase in intracellular peroxide production was detected in N-Wog- but not Wog-treated HL-60 cells by the DCHF-DA assay, and the reduction of intracellular peroxide by catalase (CAT) induced by N-Wog significantly reduced the N-Wog- but not the Wog-induced cytotoxic effect according to the MTT assay in accordance with the blocking of DNA ladder formation and caspase 3 and PARP protein processing elicited by N-Wog. Peroxides 176-184 catalase Homo sapiens 188-196 17955493-5 2008 Interestingly, an increase in intracellular peroxide production was detected in N-Wog- but not Wog-treated HL-60 cells by the DCHF-DA assay, and the reduction of intracellular peroxide by catalase (CAT) induced by N-Wog significantly reduced the N-Wog- but not the Wog-induced cytotoxic effect according to the MTT assay in accordance with the blocking of DNA ladder formation and caspase 3 and PARP protein processing elicited by N-Wog. Peroxides 176-184 catalase Homo sapiens 198-201 18344119-6 2008 This was proved to be substantially attributed to the catalase-dependent breakdown of NO(*), which was stimulated by some of peroxides (most probably being H(2)O(2)), the dismutation products of tar particulate matters (TPM). Peroxides 125-134 catalase Homo sapiens 54-62 18063869-2 2008 Erythrocyte catalase (CAT) and cellular glutathione peroxidase (c-GPx) are antioxidant enzymes that detoxify peroxides generated from dismutation of superoxide anion. Peroxides 109-118 catalase Homo sapiens 22-25 17329258-4 2007 The protein was highly susceptible to oxidation by adventitious peroxide, which could be prevented by treating buffers with low concentrations of catalase. Peroxides 64-72 catalase Homo sapiens 146-154 15892615-8 2005 Catalase is not able to destroy methemoglobin-peroxide complexes, but it can prevent their production in the course of interaction of methemoglobin and free peroxide by destroying the latter. Peroxides 46-54 catalase Homo sapiens 0-8 17305120-3 2007 Hydrogen peroxide in aqueous solutions of varying pH, temperature and concentration was continuously removed through a reactor containing the catalase-entrapped chitosan beads at high efficiency for 24 h. Additional silicate coating of the chitosan beads resulted in significant improvements in the catalase performance under harsh conditions, which are often found in peroxide-based industrial processes. Peroxides 9-17 catalase Homo sapiens 142-150 17305120-3 2007 Hydrogen peroxide in aqueous solutions of varying pH, temperature and concentration was continuously removed through a reactor containing the catalase-entrapped chitosan beads at high efficiency for 24 h. Additional silicate coating of the chitosan beads resulted in significant improvements in the catalase performance under harsh conditions, which are often found in peroxide-based industrial processes. Peroxides 9-17 catalase Homo sapiens 299-307 16632121-6 2006 On the other hand, ascorbate could decrease toxicity by converting highly reactive singlet oxygen to less reactive hydrogen peroxide, which can be removed via peroxide-removing systems such as glutathione and catalase. Peroxides 124-132 catalase Homo sapiens 209-217 16226717-7 2005 This contrasts sharply with the P450-catalyzed reaction, which is brought about by iron-bound peroxide that is inaccessible to catalase. Peroxides 94-102 catalase Homo sapiens 127-135 15892615-8 2005 Catalase is not able to destroy methemoglobin-peroxide complexes, but it can prevent their production in the course of interaction of methemoglobin and free peroxide by destroying the latter. Peroxides 157-165 catalase Homo sapiens 0-8 15241731-9 2004 As one possible mechanism, we have recently found altered expression of catalase in IGFBP-2-overexpressing tumor cells, thus implicating IGFBP-2 in influencing intracellular peroxide levels. Peroxides 174-182 catalase Homo sapiens 72-80 16403980-5 2005 We show that MAPK kinase pathway is involved in homocysteine induced DNA synthesis and proliferation of vascular smooth muscle cells in the presence of the peroxide scavenging enzyme, catalase. Peroxides 156-164 catalase Homo sapiens 184-192 16083140-4 2005 The CBA dose half effect concentration-inhibition rate of two antioxidant enzyme activity superoxide dismutase (SOD) and catalase (CAT) had the quadratic relationship, and CBA dose-inhibition rate of the peroxides (POD) activity had the linear relationship (p < 0.05). Peroxides 204-213 catalase Homo sapiens 131-134 12867337-3 2003 In contrast, quenching of peroxide with catalase is a simple procedure. Peroxides 26-34 catalase Homo sapiens 40-48 10973925-5 2000 Catalase, a peroxide scavenger, suppressed bystander killing, suggesting that hydrogen peroxide generated by apoptotic cells is the death signal. Peroxides 12-20 catalase Homo sapiens 0-8 11178967-9 2001 Taken together, the paradoxical increase in the sensitivity of an MRP-overexpressing AML-2/DX100 in response to peroxides and paraquat is due to the down-regulation of catalase gene expression, which totally independent of overexpression of MRP. Peroxides 112-121 catalase Homo sapiens 168-176 12595091-0 2003 Hydrogen-peroxide-induced heme degradation in red blood cells: the protective roles of catalase and glutathione peroxidase. Peroxides 9-17 catalase Homo sapiens 87-95 12543247-1 2003 We hypothesized that inhibitors of peroxide removal, such as BCNU, an indirect inhibitor of glutathione peroxidase (GPx), and 3-amino-1,2,4-triazole (AT), a direct inhibitor of catalase (CAT), should cause toxicity to cancer cells after manganese superoxide dismutase (MnSOD) overexpression due to elevated peroxide levels. Peroxides 35-43 catalase Homo sapiens 177-185 12543247-1 2003 We hypothesized that inhibitors of peroxide removal, such as BCNU, an indirect inhibitor of glutathione peroxidase (GPx), and 3-amino-1,2,4-triazole (AT), a direct inhibitor of catalase (CAT), should cause toxicity to cancer cells after manganese superoxide dismutase (MnSOD) overexpression due to elevated peroxide levels. Peroxides 35-43 catalase Homo sapiens 187-190 12543247-1 2003 We hypothesized that inhibitors of peroxide removal, such as BCNU, an indirect inhibitor of glutathione peroxidase (GPx), and 3-amino-1,2,4-triazole (AT), a direct inhibitor of catalase (CAT), should cause toxicity to cancer cells after manganese superoxide dismutase (MnSOD) overexpression due to elevated peroxide levels. Peroxides 249-257 catalase Homo sapiens 177-185 14757978-12 2003 We show that homocysteine induces DNA synthesis and proliferation of vascular smooth muscle cells in the presence of peroxide scavenging enzyme, catalase. Peroxides 117-125 catalase Homo sapiens 145-153 12414324-0 2002 Study of catalase electrode for organic peroxides assays. Peroxides 40-49 catalase Homo sapiens 9-17 12414324-1 2002 The catalytic activity of immobilized catalase (EC 1.11.1.6) for two model peroxide compounds (dibenzoyl peroxide and 3-chloroperoxibenzoic acid) in a non-aqueous medium was used to prepare an organic-phase enzyme electrode (OPEE). Peroxides 75-83 catalase Homo sapiens 38-46 10724328-5 2000 We exposed these microsomes to superoxide which was generated using xanthine plus xanthine oxidase and catalase to prevent accumulation of peroxide due to superoxide dismutation. Peroxides 33-41 catalase Homo sapiens 103-111 10873158-3 2000 Both nuclear translocation of NF-kappaB and enhanced kappaB-dependent transcription induced by V(IV) were inhibited by overexpression of catalase, but not Cu,Zn superoxide dismutase (Cu,Zn-SOD), indicating that peroxides rather than superoxides initiated signaling. Peroxides 211-220 catalase Homo sapiens 137-145 10873158-7 2000 Overexpression of catalase, but not Cu,Zn-SOD, inhibited p38 activation, indicating that peroxides activated p38. Peroxides 89-98 catalase Homo sapiens 18-26 11229447-5 1999 We observed that 1.0 mM homocysteine induces DNA synthesis by 1.5-fold and proliferation of vascular smooth muscle cells two-fold in the presence of peroxide scavenging enzyme, catalase (2,600 U/ml). Peroxides 149-157 catalase Homo sapiens 177-185