Showing papers on "Catalase published in 1988"
TL;DR: Using a new approach, the peroxidatic function of catalase is exploited for the determination of enzyme activity and it was successfully applied to microgram amounts of mouse liver and pancreatic islet homogenates.
909 citations
TL;DR: Salin et al. as discussed by the authors reviewed the production of oxyradicals and intermediates by chloroplasts as well as the means of protection are discussed in this review and concluded that these highly reactive intermediates pose the threat of toxicity unless neutralized by scavenger substrates or enzymes.
Abstract: Salin, M. L. 1988. Toxic oxygen species and protective systems of the chloroplast. -Physiol. Plant. 72: 681–689.
As a consequence of living in an environment enriched in oxygen, which they themselves at least partially generate, photosynthetic organisms are exposed to large fluxes of oxyradicals and reactive oxygen species. Among these are superoxide, hydrogen peroxide, hydroxyl radical and singlet oxygen. These highly reactive intermediates pose the threat of toxicity unless neutralized by scavenger substrates or enzymes. The production of oxyradicals and intermediates by chloroplasts as well as the means of protection are discussed in this review.
455 citations
TL;DR: PEG conjugation to superoxide dismutase and catalase enhances cell association of these enzymes in a manner which increases cellular enzyme activities and provides prolonged protection from partially reduced oxygen species.
438 citations
TL;DR: Three possible sources have been identified for the production of active oxygen species: the enzyme xanthine oxidase; the activated polymorphonuclear leukocyte; the disrupted mitochondrial electron transport system.
283 citations
TL;DR: It is concluded that isolated human plasma from healthy subjects is very unlikely to contain hydrogen peroxide in concentrations greater than about 0.25 microM and does not contain lipid hydroperoxides in concentrations less than 0.03 microM.
258 citations
TL;DR: Hydrogen peroxide steady state levels of 5 micromolar were determined in soybean (Glycine max) embryonic axes incubated for 2 hours and in axes pretreated with aminotriazole or cyanide, where these levels were 50 and 1micromolar, respectively.
Abstract: Hydrogen peroxide steady state levels of 5 micromolar were determined in soybean (Glycine max) embryonic axes incubated for 2 hours and in axes pretreated with aminotriazole or cyanide, where these levels were 50 and 1 micromolar, respectively. The activities of catalase (105 picomoles H(2)O(2) per minute per axis), peroxidase (10-44 picomoles H(2)O(2) per minute per axis), glutathione peroxidase (3 picomoles H(2)O(2) per minute per axis) and superoxide dismutase (3.5 units per axis), were also determined. Catalase seems to be the most important H(2)O(2) consuming enzyme at the physiological concentration of H(2)O(2). A short treatment with aminotriazole, while substantially increasing H(2)O(2) level, did not affect the growth of the axes. The production of superoxide anion by the mitochondria isolated from soybean axes was measured from the superoxide dismutase-sensitive rate of adrenochrome formation in the presence of NADH or succinate as substrate and amounted to 1.3 and 0.8 nanomole O(2) (-) per minute per milligram protein, respectively. According to the stoichiometry of O(2) (-) and H(2)O(2) dismutation reactions, it is apparent that about 0.9 to 1.5% of the total oxygen uptake proceeds through the formation of the free intermediates of the partial reduction of oxygen.
183 citations
TL;DR: The present results suggest that superoxide free radicals are involved in the development of ethanol-induced gastric mucosal lesions, probably via an interaction with cellular membranes.
Abstract: The involvement of oxygen free radicals in the development of the ethanol-induced gastric mucosal damage has been investigated. We found that oral administration of superoxide dismutase reduced the incidence of ethanol-induced mucosal lesions. Reduction of superoxide dismutase activity by diethyldithiocarbamate led to a pronounced aggravation of mucosal damage. Inhibition of the chloride-bicarbonate channel by a stilbene derivative also aggravated the ethanol-induced hemorrhagic lesions. Neither glutathione peroxidase, catalase, nor ceruloplasmin were capable of inhibiting the development of mucosal damage. Compounds with scavenging properties such as thiourea, 1-phenyl-3-(2-thiazolyl)-2-thiourea, dimethyl sulfoxide, various inorganic compounds (elements of the first and second subgroups and of the sixth group of the periodic table) and sulfhydrylcontaining substances protected the gastric mucosa against ethanol-induced injury in a dose-related manner. Naturally occurring antioxidants such as α-tocopherol, β-carotene, and coenzyme Q10 were ineffective. The present results suggest that superoxide free radicals are involved in the development of ethanol-induced gastric mucosal lesions, probably via an interaction with cellular membranes.
160 citations
TL;DR: It was found that in the honeys with high antibacterial activity a large part of this activity was due to a factor other than hydrogen peroxide, suggesting that the non-peroxide antib bacterial activity is of floral origin.
Abstract: SummaryA range of New Zealand monofloral honeys was assayed for antibacterial activity with and without the hydrogen peroxide present (inactivated by the addition of catalase). It was found that in the honeys with high antibacterial activity a large part of this activity was due to a factor other than hydrogen peroxide. The test micro-organism used, Staphylococcus aureus, was not inhibited by the osmolarity or the acidity of the honey. The association of high antibacterial activity with particular floral sources suggests that the non-peroxide antibacterial activity is of floral origin. The activity of manuka honey was tested and found to be heat-stable.
156 citations
TL;DR: The role of oxygen radicals are demonstrated in causing inactivation of Ca2+-ATPase and inhibition of lipid peroxidation of the sarcoplasmic reticulum which could possibly be one of the important mechanisms of oxygen radical-mediated myocardial injury.
138 citations
TL;DR: Current knowledge on the biochemistry of oxygen toxicity in general and the is-chemia-reoxygenation tissue injury in particular is summarized.
Abstract: This paper summarizes current knowledge on the biochemistry of oxygen toxicity in general and the ischemia-reoxygenation tissue injury in particular. The superoxide radical, hydrogen peroxide, and the hydroxyl radical in cells can be formed enzymically or nonenzymically. Primary effects of oxygen radicals result in lipid peroxidation, which is believed to be initiated by a perferryl radical. Secondary effects are believed to be due to a disturbance in cellular calcium homeostasis. Reactions and treatment potentials are highly complex and their effects on cells, tissues, and organism are difficult to predict. Treatment potentials include superoxide dismutase, catalase, calcium entry blockers, iron chelators, xanthine oxidase inhibitors, and agents to prevent leukocyte adhesion. Reoxygenation injury mechanisms during resuscitation from clinical death can be studied in animals by evaluating the effects of antireoxygenation injury therapies and by monitoring free radical reactions.
135 citations
TL;DR: It is suggested that H2O2-inactivated SOD is recognized and preferentially degraded by the same ATP-independent, metallo- serine- and sulfhydryl- proteinase pathway which degrades other oxidatively denatured red cell proteins.
TL;DR: The results obtained indicate that the peroxisomal catalases compared have very similar three-dimensional structures and might have similar targeting signals.
Abstract: The nucleotide sequence of a 2785-base-pair stretch of DNa containing the Saccharomyces cerevisiae catalase A (CATI) gene has been determined. This gene contains an uninterrupted open reading frame encoding a protein of 515 amino acids (relative molecular mass 58490). Catalase A, the peroxisomal catalase of S. cerevisiae was compared to the peroxisomal catalases from bovine liver and from Candida tropicalis and to the non-peroxisomal, presumably cytoplasmic, catalase T of S. cerevisiae. Whereas the peroxisomal catalases are almost colinear, three major insertions have to be introduced in the catalase T sequence to obtain an optimal fit with the other proteins. Catalase A is most closely related tothe C. tropicalis enzyme. It is also more similar to the bovine liver catalase than to the second S. cerevisiae catalase. The differences between the two S. cerevisiae enzymes are most striking within four blocks of amino acids consisting of a total of 37 residues with high homology between the three peroxisomal, but low conservation betwen the S. cerevisiae catalases. The results obtained indicate that the peroxisomal catalases compared have very similar three-dimensional structures and might have similar targetting signals.
TL;DR: Juvenile and adult S. mansoni show differences in susceptibility to in vitro oxidant killing that correlate with differences in their levels of endogenous antioxidants.
TL;DR: H2O2-pretreated cells had the ability to rapidly recover both proton motive force-dependent and -independent transport and required transcription and translation and was dependent on oxyR+ and katG+, providing evidence that these genes play crucial roles in the rapid recovery of transport.
Abstract: Different conditions of oxidative stress were used to study their effects on membrane transport in Escherichia coli K-12. The oxidizing conditions included H2O2, plumbagin (a redox cycling compound that generates superoxide radicals [O2-]), and increased partial pressure of oxygen. Both superoxide radical-generating conditions and H2O2 treatments were found to cause a rapid decrease in proton motive force-dependent and -independent transport. H2O2-pretreated cells had the ability to rapidly recover both proton motive force-dependent and -independent transport. The induction required transcription and translation and was dependent on oxyR+ and katG+, providing evidence that these genes play crucial roles in the rapid recovery of transport. The effects of oxidatively induced loss of proton motive force on cell growth and macromolecular synthesis were also investigated.
TL;DR: The ovothiol system is more effective than egg catalase in destroying H2O2 at concentrations produced during fertilization and constitutes a principal mechanism for preventing oxidative damage at fertilization.
Abstract: Despite its potential toxicity, H2O2 is used as an extracellular oxidant by Stronglylocentrotus purpuratus eggs to cross-link their fertilization envelopes. These eggs contain 5 mM 1-methyl-N alpha,N alpha-dimethyl-4-mercaptohistidine (ovothiol C), which reacts with H2O2. In consuming H2O2 and being reduced by glutathione, ovothiol acts as a glutathione peroxidase and replaces the function of the enzyme in eggs. The ovothiol system is more effective than egg catalase in destroying H2O2 at concentrations produced during fertilization and constitutes a principal mechanism for preventing oxidative damage at fertilization.
TL;DR: It is concluded that the antiproliferative action of gliotoxin may be caused by DNA damage effected by reactive oxygen species or other radicals generated through redox cycling.
TL;DR: H2O2 is the major cytotoxic product formed by the xanthine/xanthine oxidase system, and it is concluded that cells exposed to this system in phosphate-buffered saline or serum-containing medium were affected by this product.
Abstract: 1. The survival of mammalian epithelial cells exposed in vitro to the xanthine/xanthine oxidase system in phosphate-buffered saline (PBS) or serum-containing medium (SCMEM) was investigated. 2. The cytotoxic effect observed depended on the composition of the medium in which the enzymic reaction was carried out; a surviving fraction of 5 x 10(-5) was found for cells exposed in PBS and 5.2 x 10(-1) for those in SCMEM. 3. The cytotoxic product(s) formed by the xanthine/xanthine oxidase system was relatively stable in PBS; survival of cells incubated after completion of the enzymic reaction was always less than that found for cells exposed during the reaction in the same system. 4. Superoxide dismutase or mannitol present during the enzymic reaction did not inhibit the cytotoxic effect. 5. NaN3 (a single-oxygen quencher and a catalase inhibitor) added to the system in SCMEM caused a reduction in survival to the level observed for cells exposed to the enzymic reaction in PBS. 6. Catalase completely protected cells, but no protection was observed when both catalase and NaN3 were present in the reaction mixture. 7. A similar cytotoxic effect was produced when cells were treated with H2O2 alone. 8. The rate of H2O2 decomposition in medium was accelerated by the presence of serum, but this was completely inhibited by NaN3. 9. It is concluded that H2O2 is the major cytotoxic product formed by the xanthine/xanthine oxidase system.
TL;DR: These findings underscore the importance of macrophages in EAN and provide evidence that, in this model, macrophagederived reactive oxygen intermediates contribute to damage of the myelin sheath.
Abstract: Macrophages have been implicated in myelin damage in experimental autoimmune neuritis (EAN). We examined a possible pathogenetic role of toxic oxygen species elaborated by macrophages in EAN by administering oxygen radical scavengers. Early treatment of rats with either catalase or superoxide dismutase (10,000 U/kg/day) protected animals from the development of EAN. Treatment delayed until there was clinical manifestation of EAN (day 13) still markedly attenuated the severity of the disease, as evidenced by clinical assessment, electrophysiological studies, and morphological observation. In cell culture, macrophages from sham-treated controls generated heightened oxidative metabolic responses indicating in vivo macrophage activation. Addition of catalase or superoxide dismutase abrogated or diminished chemiluminescence and production of reactive oxygen intermediates by macrophages ex vivo. Our findings underscore the importance of macrophages in EAN and provide evidence that, in this model, macrophage-derived reactive oxygen intermediates contribute to damage of the myelin sheath.
TL;DR: Evidence is presented that Saccharomyces cerevisiae can metabolize fatty acids via the inducible peroxisomal beta-oxidation pathway even when these acids are not the sole carbon source.
Abstract: The regulation of synthesis of haemoproteins in Saccharomyces cerevisiae provides an excellent model system for studying the mechanisms of coordinated control of gene expression. Our interest in this problem is of long standing [l - 51. For present studies we have chosen catalases as model proteins. In S. cerevisiue there are two catalases: T, typical and A, atypical [6]. Synthesis of both enzymes depends on availability of haem, oxygen tension and glucose concentration in the medium, synthesis of catalase A being more sensitive to glucose repression [2, 71. A number of mutants with altered regulation of catalase T synthesis have been isolated but none of the mutations affected catalase A. The properties of the mutants indicate that the expression of genes coding for catalase T and A is controlled independently. The two enzymes differ also in their localization in the cell; catalase T is a cytoplasmic enzyme, whereas catalase A appears to be an organelle-bound one [8, 91. On the other hand it is known that in some yeast species the growth on unusual carbon and nitrogen sources, such as methanol, paraffins, long-chain fatty acids, monoamines and polyamines, D-aminO acids or uric acid, leads to induction of the appropriate oxidases [lo- 161. These enzymes are localized in peroxisomes and oxidize their substrates by reducing oxygen to hydrogen peroxide. In all cases the activity of hydrogen-peroxide-producing oxidases is accompanied by increased activity of catalase, decomposing the generated hydrogen peroxide. This prompted us to examine whether
01 Jan 1988
TL;DR: The results indicate that the calorigenic response in the hyperthyroid state is accompanied by the development of an hepatic oxidative stress characterized by enhanced spontaneous chemiluminescence, enhanced NADPH-dependent microsomal respiration and a decreased antioxidant cellular activity.
Abstract: Chemiluminescent and respiratory responses were studied in the liver of rats treated with 0.1 mg of triiodothyronine (T3)/kg for 1 to 7 days. Hyperthyroidism resulted in significant increments in the spontaneous chemiluminescence of the in situ liver in animals exhibiting a calorigenic response. Microsomal NADPH-dependent oxygen uptake was enhanced by T3 treatment for 2 days, an effect that was completely abolished by the antioxidant cyanidanol. A similar microsomal antioxidant-sensitive respiratory component was observed in this situation after the addition of t-butyl hydroperoxide (t-BHP). However, basal rates of microsomal oxygen uptake and light emission in liver homogenates and microsomes were decreased by t-BHP, probably related to thyroid hormone-induced diminution in the content of cytochrome P-450 (Fernandez et al.) In addition, liver superoxide dismutase and catalase activities as well as the total content of glutathione were depressed by T3. These results indicate that the calorigenic response in the hyperthyroid state is accompanied by the development of an hepatic oxidative stress characterized by enhanced spontaneous chemiluminescence, enhanced NADPH-dependent microsomal respiration and a decreased antioxidant cellular activity.
TL;DR: A new fungal catalase is purified and characterized, with a molecular weight of 215,000 and a pI of 5.5 for this enzyme.
Abstract: We purified and characterized a new fungal catalase. The specific activity of the preparation obtained is 1500 Ul/mg of protein. We found a molecular weight of 215, 000 and a pl of 5. 5 for this enzyme.
TL;DR: In this article, growth inhibition of Escherichia coli in the presence of 2-bromo-2-nitropropane-1,3-diol (bronopol) indicate a period of biocide-induced bacteriostasis followed by growth at an inhibited rate.
Abstract: Patterns of growth inhibition of Escherichia coli in the presence of 2-bromo-2-nitropropane-1,3-diol (bronopol) indicate a period of biocide-induced bacteriostasis followed by growth at an inhibited rate. The length of the bacteriostatic period, but not the subsequent growth inhibition, was reduced by the addition of excess cysteine. Patterns of growth inhibition were unaffected by catalase or superoxide dismutase. The bactericidal concentrations (100 to 500 micrograms/ml) were considerably in excess of the MIC (13 micrograms/ml) and generally produced first-order reductions in viability. Bactericidal activity was considerably reduced by anoxic conditions and by the presence of catalase or superoxide dismutase. Results indicate that there are two distinct reactions between bronopol and thiols. Under aerobic conditions, bronopol catalytically oxidizes thiol-containing materials such as cysteine, with atmospheric oxygen as the final oxidant. By-products of this reaction are active oxygen species such as superoxide and peroxide, which are directly responsible for the bactericidal activity of the compound and for the reduced growth rate after the bacteriostatic period. The latter effect probably results from the oxidation of intracellular thiols such as glutathione and cysteine. Catalytic oxidation of thiols in the presence of excess thiol leads to the creation of an anoxic state. Under these conditions, the slower reaction with thiols, which consumes bronopol, predominates. Consumption of bronopol by its reaction with thiols, without the involvement of oxygen, leads to the eventual removal of bronopol from treated suspensions and the resumption of growth.
TL;DR: The NADPH-supported enzymatic reduction of molecular oxygen by ferredoxin-ferredoxin:NADP+ oxidoreductase was investigated and Catalase was shown to inhibit formation of the hydroxyl radical adduct, further supporting the formation of hydrogen peroxide as an intermediate during the reduction of oxygen.
TL;DR: Superoxide dismutase/catalase markedly improved the PAF-induced lesions, indicating that most of the intestinal damage after PAF injection is because of the release of oxygen radicals.
Abstract: The mechanism of tissue and cell injury in ischaemic bowel necrosis is unclear. The present study investigated the role of oxygen derived free radicals in the development of bowel necrosis using injections of platelet activating factor (PAF) into the mesenteric vasculature. Animals were pretreated with allopurinol or superoxide dismutase together with catalase, before administration of PAF. Superoxide dismutase/catalase markedly improved the PAF-induced lesions, indicating that most of the intestinal damage after PAF injection is because of the release of oxygen radicals. The major source of oxygen radicals is xanthine oxidase, as allopurinol ameliorated small bowel lesions. Pretreatment with allopurinol produced a significant (p less than 0.01) preventive effect on PAF induced hypotension. In contrast, superoxide dismutase/catalase did not alter PAF induced hypotension. Superoxide dismutase/catalase pretreatment improved PAF induced haemoconcentration and leucopenia, while allopurinol showed no effect.
TL;DR: The results strongly indicate that the 64,000-Mr protein (catalase?) is not a precursor to the 57, thousands-Mr catalase and that cottonCatalase is translated on cytosolic ribosomes without a cleavable transit or signal sequence.
Abstract: As part of our research on peroxisome biogenesis, catalase was purified from cotyledons of dark-grown cotton (Gossypium hirsutum L.) seedlings and monospecific antibodies were raised in rabbits. Purified catalase appeared as three distinct electrophoretic forms in non-denaturing gels and as a single protein band (with a subunit Mr of 57,000) on silver-stained SDS/polyacrylamide gels. Western blots of crude extracts and isolated peroxisomes from cotton revealed one immunoreactive polypeptide with the same Mr (57,000) as the purified enzyme, indicating that catalase did not undergo any detectable change in Mr during purification. Synthesis in vitro, directed by polyadenylated RNA isolated from either maturing seeds or cotyledons of dark-grown cotton seedlings, revealed a predominant immunoreactive translation product with a subunit Mr of 57,000 and an additional minor immunoreactive product with a subunit Mr of 64000. Labelling studies in vivo revealed newly synthesized monomers of both the 64000- and 57,000-Mr proteins present in the cytosol and incorporation of both proteins into the peroxisome without proteolytic processing. Within the peroxisome, the 57,000-Mr catalase was found as an 11S tetramer; whereas the 64,000-Mr protein was found as a relatively long-lived 20S aggregate (native Mr approx. 600,000-800,000). The results strongly indicate that the 64,000-Mr protein (catalase?) is not a precursor to the 57,000-Mr catalase and that cotton catalase is translated on cytosolic ribosomes without a cleavable transit or signal sequence.
TL;DR: The results suggest that adaptation to chronic oxidative stress mediated by H2O2 in mammalian cells is accompanied by a stable heritable change in expression of catalase activity.
Abstract: Hydrogen peroxide (H2O2)-resistant variants of the Chinese hamster ovary HA-1 line have been derived by culturing cells in progressively higher concentrations of H2O2 (greater than 200 days, in 50-800 microM H2O2). The H2O2-resistant phenotype has been stable for over 60 passages (240 days) following removal from the H2O2 stress. The resistant cells demonstrate both increased capacity to deplete exogenously added H2O2 from the growth medium and increased catalase activity. H2O2 resistance correlates well with catalase activity. An increase in chromosome number occurred in the cells adapted to 200-800 microM H2O2, but increases in aneuploidy and tetraploidy were not necessary for resistance. These results suggest that adaptation to chronic oxidative stress mediated by H2O2 in mammalian cells is accompanied by a stable heritable change in expression of catalase activity.
TL;DR: Catalase-negative mutant of the yeast Hansenula polymorpha consumed methanol in the presence of glucose when the organism was grown in carbon-limited chemostat cultures, and cytochrome c peroxidase is a key enzyme of H(2)O( 2) detoxification in yeasts.
Abstract: A catalase-negative mutant of the yeast Hansenula polymorpha consumed methanol in the presence of glucose when the organism was grown in carbon-limited chemostat cultures. The organism was apparently able to decompose the H(2)O(2) generated in the oxidation of methanol by alcohol oxidase. Not only H(2)O(2) generated intracellularly but also H(2)O(2) added extracellularly was effectively destroyed by the catalase-negative mutant. From the rate of H(2)O(2) consumption during growth in chemostat cultures on mixtures of glucose and H(2)O(2), it appeared that the mutant was capable of decomposing H(2)O(2) at a rate as high as 8 mmol . g of cells . h. Glutathione peroxidase (EC 1.11.1.9) was absent under all growth conditions. However, cytochrome c peroxidase (CCP; EC 1.11.1.5) increased to very high levels in cells which decomposed H(2)O(2). When wild-type H. polymorpha was grown on mixtures of glucose and methanol, the CCP level was independent of the rate of methanol utilization, whereas the level of catalase increased with increasing amounts of methanol in the substrate feed. Also, the wild type decomposed H(2)O(2) at a high rate when cells were grown on mixtures of glucose and H(2)O(2). In this case, an increase of both CCP and catalase was observed. When Saccharomyces cerevisiae was grown on mixtures of glucose and H(2)O(2), the level of catalase remained low, but CCP increased with increasing rates of H(2)O(2) utilization. From these observations and an analysis of cell yields under the various conditions, two conclusions can be drawn. (i) CCP is a key enzyme of H(2)O(2) detoxification in yeasts. (ii) Catalase can effectively compete with mitochondrial CCP for hydrogen peroxide only if hydrogen peroxide is generated at the site where catalase is located, namely in the peroxisomes.
TL;DR: Cells pretreated with xanthine-xanthine oxidase are less mutated than control cultures when challenged with ionizing radiation and the rate of DNA single-strand breaks rejoining in cells challenged with H2O2 or gamma-rays is not modified.
Abstract: Pretreatment of Chinese hamster ovary (CHO) or H4 (rat hepatoma) cells with low non-toxic doses of H 2 O 2 or xanthine-xanthine oxidase renders the cells more resistant to the toxic effect of H 2 O 2 and γ-rays. This increased resistance is observed both in exponentially growing and in plateau-phase cells. Cells pretreated with xanthine-xanthine oxidase are less mutated than control cultures when challenged with ionizing radiation. The number of DNA single-strand breaks (measured by nucleoid sedimentation) induced by a high dose of γ-rays or H 2 O 2 is lower in cells pretreated with xanthine-xanthine oxidase compared to control cultures. However, the pretreatment does not modify the rate of DNA single-strand breaks rejoining in cells challenged with H 2 O 2 or γ-rays. The catalase activity is not modified in pretreated cells, but the superoxide dismutase activity is increased about 2-fold.