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At least 433 records · Page 24Linked to original sources
PubMed2004

Age-related changes in superoxide dismutase, glutathione peroxidase, catalase and xanthine oxidoreductase/xanthine oxidase activities in the rabbit cornea.

The activities of superoxide dismutase, glutathione peroxidase (GPX) and catalase--the enzymatic scavengers of reactive oxygen species and the activities of xanthine oxidoreductase and xanthine oxidase, an enzyme known to generate reactive oxygen species, were studied in the corneas of normal rabbit eyes of various ages (1 month--young eyes; 4-9.5 months--young adult eyes; 2.0-2.75 years--middle aged eyes; 3.0-5.0 years--aged eyes). The activities of GPX, superoxide dismutase, xanthine oxidoreductase and xanthine oxidase were investigated biochemically in the scraped corneal epithelium. Catalase activity was detected histochemically in the corneal epithelium and endothelium. The results show that young corneas revealed lower activities of all the antioxidant enzymes investigated than did young adult corneas, in which enzymatic activities reached their maximum. In middle-aged corneas, GPX and catalase activities remained approximately at the same levels as seen in young adult corneas, whereas superoxide dismutase activity was decreased. In aged corneas, the activities of all antioxidant enzymes were dramatically decreased or even lost (catalase activity in the corneal endothelium). In contrast, xanthine oxidoreductase activity only slightly decreased with age and the xanthine oxidase proportion of total xanthine oxidoreductase remained unchanged. GPX, superoxide dismutase and catalase are important antioxidant enzymes protecting the cornea against the oxidative damage. Because the activities of these enzymes are lower in young animals and greatly reduced in aged animals, it is suggested that young and particularly aged corneas might be more susceptible to oxidative stress than are young adult corneas. This presumption is supported by the fact that the activities of prooxidant enzymes (xanthine oxidoreductase/xanthine oxidase) are only slightly decreased in aged corneas as compared to young adult corneas so that some imbalance between antioxidant and prooxidant enzymes exists already in the normal aged corneas.

Aging↗
PubMed2003

Metabolic and biochemical responses of probiotic bacteria to oxygen.

The interaction between oxygen and probiotic bacteria was studied by growing Lactobacillus acidophilus and Bifidobacterium spp. in 0, 5, 10, 15, and 21% oxygen in a hypoxic glove box. The metabolic responses of each probiotic strain in the different oxygen environments were monitored by measuring the levels of lactic acid and determining the lactate-to-acetate ratio. Biochemical changes induced by oxygen were examined by monitoring the specific activities of NADH oxidase, NADH peroxidase, and superoxide dismutase. In addition, the ability to decompose hydrogen peroxide and the sensitivity of each strain to hydrogen peroxide was also determined. With an increase in oxygen percentage, levels of lactic acid in L. acidophilus strains decreased, whereas the lactate-to-acetate ratio reduced in all the bifidobacteria tested. At 21% oxygen, the specific activities of NADH oxidase and NADH peroxidase, and the hydrogen peroxide decomposing ability of five probiotic strains was significantly higher than at 0% oxygen. The sensitivity of the probiotic strains to hydrogen peroxide however, remained unaffected in all the different oxygen percentages. Superoxide dismutase levels did not reveal any conclusive trend. In both L. acidophilus and Bifidobacterium spp., NADH oxidase and NADH peroxidase functioned optimally at pH 5. Growth in the various oxygen environments did not change this optimum pH.

Bifidobacterium↗
PubMed1979

Cell-density-dependent Changes in the Metabolism of Chloronema Cell Cultures: I. Relationship between Cell Density and Enzymic Activities.

In the growing chloronema cell suspension cultures of the moss Funaria hygrometrica Hedw., activities of several enzymes have been found to be cell-density-dependent. Cyclic nucleotide phosphodiesterase (cNPDE), nitrate reductase (NR), and protein kinase showed highest activity at a low cell density (1 to 2 milligrams per milliliter) while indoleacetic acid (IAA) oxidase and peroxidase were highest at a high cell density (>10 milligrams per milliliter). 3'-Nucleotidase and the glycolytic enzymes (aldolase, hexokinase, phosphofructokinase, phosphoglucoisomerase, pyruvate kinase, and triose phosphate isomerase) showed no significant dependence on the cell density. Alternatively, if the NR and peroxidase activities were determined as a function of time in batch cultures, their levels were maximal 60 to 70 and 320 hours after subculture, respectively, the corresponding cell densities being 1 to 2 and 23 milligrams per milliliter. The relationship between cell density and NR and peroxidase activities is the same, whether these enzymes are measured in batch cultures during a growth cycle or in the cells cultured at different initial inoculum densities for a constant time. Conventionally enzymic changes have been correlated with growth phases; however, it is felt that the pattern of enzymic activities can also be interpreted as cell-density-dependent.In moss protonema, the dependence of cNPDE, IAA oxidase, and peroxidase on cell density may play an important role in modulating the endogenous levels of IAA and cAMP, both of which regulate the differentiation of specific cell types (Johri and Desai 1973 Nature New Biol 245: 223-224; and Handa and Johri 1976 Nature 259: 480-482).

Journal Article↗
PubMed1992

Enzyme packed bed system for the on-line measurement of glucose, glutamate, and lactate in brain microdialysate.

Rapid measurement of glucose, glutamate, and lactate is important in understanding the dynamics of the energy balance of the brain. Glutamate is also the main excitatory neurotransmitter. A general immobilized enzyme-based flow injection assay system is described which uses oxidase and peroxidase enzymes to convert the analyte into an oxidized ferrocene species which is detected electrochemically by reduction. The enzymes glucose oxidase, glutamate oxidase, lactate oxidase, and horseradish peroxidase are immobilized with near 100% efficiency onto 10-microns tresyl-activated silica beads (1000- and 500-A pore size). The beads are slurry-packed into 2- x 20-mm columns to give beds for glucose, glutamate, or lactate which are stable for greater than 40 days. The flow injection assays described have detection limits from 1.8 to less than 20 pmol and have been configured to have linear calibration responses over the range of basal and stimulated levels of the three compounds found in 5-microL microdialysate samples from the rat striatum. The assays are used for automated on-line measurement of glucose, glutamate, and lactate in striatal microdialysate at 2.5-min intervals.

Animals↗
PubMedDate not supplied

Fractionation and characterization of two forms of peroxidase from Oryza sativa.

Peroxidase (E.C. 1.11.1.7., hydrogen donor oxidoreductase) is widely distributed and has been isolated from many higher plants (1). The wide distribution of the enzyme suggests that it could be of great biological importance. However the role that it plays in metabolism is not clear due to the large number of reactions it catalyzes and the considerable number of isozymic species (2). In tomato plants, Evans and Aldridge (3) separated out six isoperoxidases and in a later paper Evans reported 12 isoperoxidases from tomato shoots (4). A homogeneous tomato fruit peroxidase isozyme was obtained by Jen et al. (5) using hydrophobic chromatography. Isozymes were not detected in Euphorbia characias peroxidase (6), in Ipomoea batatas peroxidase (7) and in Hordeum vulgare peroxidase (8). The simultaneous presence of Cu (II) amine oxidase and peroxidase in cell walls suggests that the peroxide generated on oxidation of the amines could be utilized by the peroxidase (6,8,9). In the graminea Oryza sativa, widely distributed, an FAD amine oxidase is present that oxidizes diamines (10). In this plant we also found two isoperoxidases called perox I and II. Only perox I was purified to homogeneity and its enzymatic, physical and chemical properties have been studied.

Chemical Fractionation↗
PubMed1995

Modifications to a carbon paste glucose-sensing enzyme electrode and a reduction in the electrochemical interference from L-ascorbate.

A glucose-sensing enzyme electrode was prepared by incorporating polyethylene glycol-modified glucose oxidase, horseradish peroxidase and 1,1'-dimethylferrocene into a carbon paste. The modification of glucose oxidase with polyethylene glycol was effective for increasing the enzyme activity in the carbon paste owing to the enhanced affinity of the polyethylene glycolmodified enzyme for the hydrophobic carbon paste matrix. In contrast, however, the enzyme activity of the polymer-modified peroxidase was lower than the unmodified peroxidase in the carbon paste matrix because of a severe loss of the enzyme activity during the modification with polyethylene glycol. Hence, the enzyme pair of polyethylene glycol-modified glucose oxidase and unmodified peroxidase was used for preparing the enzyme electrode. The reductive current response of the electrode to glucose was recorded at -0.2 V vs. Ag/AgCl. After the addition of glucose (100 microM), the current increased immediately and reached a plateau (delta = -0.12 microA) within 30 s. The current response was linear up to a glucose concentration of 500 microM and the detection limit was 20 microM (S/N = 5). Interference from ascorbate was very small: the current response to 1 mM glucose (-1.1 microA) was slightly reduced to -0.9 microA when 1 mM ascorbate was added to the glucose-containing solution. In biological and food samples, the concentration of ascorbate is generally quite low compared with the glucose concentration. The interference from ascorbate could actually be ignored for the purpose of determining glucose in soft drinks.

Ascorbic Acid↗
PubMed1992

Inhibition of veratryl alcohol oxidase activity of lignin peroxidase H2 by 3-amino-1,2,4-triazole.

The oxidation of veratryl alcohol (3,4-dimethoxybenzyl alcohol) by lignin peroxidase H2 from Phanerochaete chrysosporium and H2O2 was inhibited by 3-amino-1,2,4-triazole (AT). Inhibition was found to be competitive with respect to veratryl alcohol (K1 = 18 microM) and noncompetitive with respect to H2O2. Unlike bovine lactoperoxidase, catalase, and thyroid peroxidase, AT was not a suicide (mechanism based) inhibitor for lignin peroxidase H2. Binding studies revealed that lignin peroxidase H2 catalyzed insignificant binding of [14C]AT to the enzyme. Apparently AT is a poor substrate for lignin peroxidase H2 and is only slowly oxidized to form a yellow product in the presence of H2O2. The formation of the yellow product was shown to increase with increasing concentrations of veratryl alcohol, suggesting that an intermediate in the oxidation of veratryl alcohol is able to mediate the oxidation of AT. Extensive metabolism of AT to CO2 by the white rot fungus Phanerochaete chrysosporium (approximately 60% in 30 days) was also demonstrated.

Alcohol Oxidoreductases↗
PubMedDate not supplied

[Oxidase activity of horseradish peroxidase in oxidation of the bilirubin-albumin complex].

The catalytic activity of horseradish peroxidase was investigated upon oxidation of the bilirubin-albumin complex (10(-5)-10(-4) M; BR: SA = 1: 1.5 mol/mol) by dissolved oxygen to biliverdin and other components. The process can be described by the Michaelis-Menten equation with Km = 14.4 microM and Vmax = 0.12 microM/min, if HRP = 3.1 x 10(-8) M. Oxidation is supposed to proceed in the triple complex--peroxidase: albumin: bilirubin.

Animals↗
PubMed2004

Characterization of novel dihydrothienopyridinium and thienopyridinium metabolites of ticlopidine in vitro: role of peroxidases, cytochromes p450, and monoamine oxidases.

Ticlopidine is an agent that inhibits adenosine diphosphate-induced platelet aggregation. Metabolic studies with ticlopidine have indicated that the principal routes of metabolism are N-dealkylation, N-oxidation, and oxidation of the thiophene ring. However, ticlopidine shares some structural features that are similar to those of cyclic tertiary amines such as 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine and tetrahydroisoquinolines, which are converted to neurotoxic pyridinium metabolites, via the iminium (dihydropyridinium) species. The current in vitro studies examined the potential of ticlopidine to undergo a similar conversion by cytochrome P450 (P450), peroxidases, and monoamine oxidase (MAO). The results from these studies have suggested that ticlopidine undergoes an overall 4-electron oxidation to the novel thienopyridinium metabolite (M6) via the intermediate 2-electron oxidation product, the thienodihydropyridinium metabolite (M5) by P450, horseradish peroxidase, and myeloperoxidase and, to a lesser extent, by MAO. The structures of these metabolites were characterized by liquid chromatography (LC)-tandem mass spectrometry and LC-NMR. Qualitative studies with baculovirus-expressed P450s revealed the involvement of P450 3A4 in this conversion. Interestingly, M5 was the primary metabolite in the peroxidase-mediated reactions and was quite stable to air oxidation or disproportionation. It was less electrophilic and did not form cyanide, glutathione, or N-acetylcysteine adducts. On the other hand, M6 was the major metabolite in P450-catalyzed oxidation of ticlopidine. The results from this study have revealed that in addition to metabolism of the thiophene ring of ticlopidine, the tetrahydropyridine moiety of the compound is susceptible to a 2-electron and a 4-electron oxidation like other cyclic tertiary amines.

Animals↗
PubMed1982

Iron-dependent free radical damage to DNA and deoxyribose. Separation of TBA-reactive intermediates.

1. Iron-dependent free radical damage to DNA and deoxyribose results in the formation of thiobarbituric acid (TBA) reactive intermediates. 2. These intermediates have been compared chromatographically and spectrophotometrically after incubation with the enzymes xanthine oxidase and peroxidase. 3. Loss of TBA-reactivity occurred in the bleomycin-iron(II) derived products incubated with xanthine oxidase and in a standard solution of sodium malondialdehyde incubated with peroxidase.

Animals↗