Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “OXIDASE AND PEROXIDASE”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 109 records · Page 6Linked to original sources

A hydrogen peroxide assay based on the peroxidase-oxidase reaction. Numerical simulation of the reaction mechanism.

In order to explain an assay method for H2O2, based on the horseradish peroxidase/NADH/H2O2 system, we performed a numerical simulation of this complex reaction mechanism. For this purpose, we applied a simplified version of a model designed by Yokota and Yamazaki to our experimental conditions [Yokota, K. & Yamazaki, I. (1977) Biochemistry 16, 1913-1918]. This modification leads to a kinetic behaviour of the system very similar to our experimental results when the presence of superoxide dismutase is simulated. These simulations confirm that hydrogen peroxide concentrations are proportional to the total amount of NADH oxidized. We also showed that superoxide dismutase activity can be determined by this assay method. Moreover, in samples containing superoxide dismutase and hydrogen peroxide, the simulations showed that both superoxide dismutase and hydrogen peroxide can be determined using our assay method.

Catalysis↗

Antioxidant binding of caeruloplasmin to myeloperoxidase: myeloperoxidase is inhibited, but oxidase, peroxidase and immunoreactive properties of caeruloplasmin remain intact.

The neutrophil enzyme myeloperoxidase (MPO) purposefully makes hypochlorous acid (HOCl) as part of the cells defence against microbial infections. During cell lysis, however, MPO will be released into the extracellular environment where production of HOCl, a powerful oxidant, will lead to molecular damage. Extracellular MPO binds to the copper-containing protein caeruloplasmin (Cp) and prevents MPO making HOCl. Cp has several important antioxidant functions in extracellular fluids associated with its ability to catalyse oxidation of ferrous ions and to remove peroxides. The binding of MPO to Cp did not inhibit these important extracellular antioxidant activities of Cp, but in so doing it provided additional antioxidant protection against formation of HOCl.

Antioxidants↗

Effect of interfering substances on current response of recombinant peroxidase and glucose oxidase-recombinant peroxidase modified graphite electrodes.

Graphite electrodes have been modified with different forms of horseradish peroxidase (HRP). These included native HRP, wild-type recombinant HRP, and two single-point recombinant HRP mutants, N70V and N70D. The mediator-less response of these electrodes to H2O2 was studied indicating that electrodes modified with recombinant HRP forms are more stable than those modified with native HRP. Various interfering compounds were investigated for their effect on the current response to H2O2. It was found that interferences such as acetaminophen and dopamine affected the response by mediating the electron transfer (ET) between graphite and peroxidases. The mediating behaviour manifested itself as an increased current of the electrode to H2O2. The interfering effect was less pronounced for the electrodes modified with recombinant HRPs possessing better electronic coupling with the graphite surface. The interfering behaviour of acetaminophen on the response for glucose with the bienzyme electrode containing co-immobilised glucose oxidase and HRP was mainly ascribed to mediation of ET between graphite and HRP. It was experimentally proven that a high efficiency of direct ET between graphite and recombinant HRP substantially reduces the interfering effect of acetaminophen.

Journal Article↗

Histochemical localization of cytochrome oxidase in the retina and optic tectum of normal goldfish: a combined cytochrome oxidase-horseradish peroxidase study.

Cytochrome oxidase (C.O.) was histochemically localized in the normal retina and optic tectum of goldfish in order to examine the laminar and cellular oxidative metabolic organization of these structures. In the optic tectum, C.O. exhibited a distinct laminar, regional, and cellular distribution. The laminae with highest C.O. levels were those that receive optic input, suggesting a dominant role for visual activity in tectal function. This was demonstrated by colocalizing C.O. and HRP-filled optic fibers in the same section. However, the distribution of C.O. within the optic laminae was not uniform. Within the main optic layers, the SFGS, four metabolically distinct sublaminae were distinguished and designated from superficial to deep as sublaminae a, b, c, and d. The most intense reactivity was localized within SFGSa and SFGSd, followed by SFGSb, then SFGSc. In SFGSd, intense reactivity was found to occur specifically within a class of large diameter axons and terminals that were apparently optic since these were also labeled with HRP and cobaltous lysine applied to the optic nerve. Regional C.O. differences across the tectum were also noted. Low levels were found in neurons and optic terminals along the growing immature medial, lateral, and posterior edges of tectum, but were higher at the more mature anterior pole and central regions of tectum. This suggests that the oxidative metabolic activity is initially low in newly formed tectal neurons and optic axons, but gradually increases with neuronal growth and functional axon terminal maturation. Most C.O. staining was localized within neuropil, whereas the perikarya of most tectal neurons were only lightly reactive. Only a few neuron classes, mostly the relatively larger projection neurons, had darkly reactive perikarya. In the retina, intense C.O. reactivity was localized within the inner segments of photoreceptors, the inner and outer plexiform layers, and within certain classes of bipolar and ganglion cells. The large ganglion cells in particular were intensely reactive. Like the large diameter optic terminals in SFGSd, the large ganglion cells were preferentially filled with HRP, suggesting that they may project to tectum and are the source of the darkly reactive large diameter axons and terminals in sublamina SFGSd. We propose a new scheme to describe tectal lamination that integrates laminar differences in C.O. reactivity with classical histological work.(ABSTRACT TRUNCATED AT 400 WORDS)

Animals↗

Aluminum-induced cell death of barley-root border cells is correlated with peroxidase- and oxalate oxidase-mediated hydrogen peroxide production.

The function of root border cells (RBC) during aluminum (Al) stress and the involvement of oxalate oxidase, peroxidase and H(2)O(2) generation in Al toxicity were studied in barley roots. Our results suggest that RBC effectively protect the barley root tip from Al relative to the situation in roots cultivated in hydroponics where RBC are not sustained in the area surrounding the root tip. The removal of RBC from Al-treated roots increased root growth inhibition, Al and Evans blue uptake, inhibition of RBC production, the level of dead RBC, peroxidase and oxalate oxidase activity and the production of H(2)O(2). Our results suggest that even though RBC actively produce active oxygen species during Al stress, their role in the protection of root tips against Al toxicity is to chelate Al in their dead cell body.

Aluminum↗

Polyphenol oxidase and peroxidase in fruits and vegetables.

Polyphenol oxidases and peroxidases are among the most studied enzymes in fruits and vegetables. Owing to the deleterious effects of discoloration and off-flavor formation induced by their actions, these enzymes have not ceased to be a matter of concern to food technologists, while their versatility as catalyst and their diversity as protein present a challenge to the biochemist. This article gives an account on the present state of knowledge in this field. The occurrence of polyphenol oxidases and peroxidases in food and food raw materials, and their role and importance in food processing are briefly outlined. Results of biochemical research including catalytic properties, substrate specificity, susceptibility towards pH and temperature, action of inhibitors, isolation, purification, and characteristics of the enzymes are given, with special emphasis on recent achievements based on high resolution separation and isoenzyme techniques. Finally, the behavior of polyphenol oxidase and peroxidase in selected major groups of fruits and vegetables is discussed. Some contradictions found in the literature are pointed out and some questions that have not been given the necessary attention by researchers so far are mentioned.

Basidiomycota↗

Comparison of glucose oxidase and peroxidase as labels for antibody in enzyme-linked immunosorbent assay.

Horse-radish peroxidase and glucose oxidase were each separately conjugated to identical aliquots of goat IgG containing anti-human IgG antibodies. We used a minor modification of the periodate method of Nakane and Kawaoi to covalently bind each enzyme to IgG. Glucose oxidase conjugates proved superior to peroxidase conjugates based on the following qualities. The glucose oxidase conjugates had 1) usable dilutions 2 to 10 times greater than peroxidase conjugates, 2) much lower background or control non-specific activities, and 3) nearly twice the sensitivity as expressed by absorbance change vs. change in antigen. Comparison of the antibody titers showed the glucose oxidase conjugate with 80% and the peroxidase conjugate with 20% of the original goat antibody.

Animals↗

Peroxidase-polyphenol oxidase association in Dioscorea esculenta.

A crude enzyme extract from Dioscorea esculenta var. fasiculata tissue subjected to ion exchange chromatography on DEAE-Sephadex A-50 column. This procedure resolved the extract into two main protein peaks one of which eluted through the column relatively unbound while the other protein peak which remained bound to the column was eluted with 1.0 M NaCl. Both protein peaks contained polyphenol oxidase (PPO) and peroxidase (POD) activities. The non-binding protein peak was resolved by gel filtration on Sephadex G-200 into distinct PPO and POD activities and by virtue of their apparent molecular weights of 95.5 Kd and 38.0 Kd for PPO and POD respectively were determined to be the typical enzymes. The PPO activity was completely inhibited invitro by 5 mM polyvinyl pyrrolidone (PVP). The binding protein peak was not resolved by gel filtration. It contained PPO activity which was not inhibited by PVP and a POD activity which was completely inhibited by dithiothreitol (DTT) This ionic protein peak contained 60% of total POD in the tissue, has an apparent molecular weight of 56 Kd and is suggested to be a strongly anionic peroxidase which also exhibits polyphenol oxidase activity.

Catechol Oxidase↗

Application of immobilized enzymes to clinical analyses : use of co-immobilized glucose oxidase and peroxidase in column form.

Glucose oxidase from Aspergillus niger and peroxidase from horseradish were simultaneously immobilized onto alkylamine glass beads which were then packed into a 1.5 x 20 mm column and integrated in the flow system of an AutoAnalyzer I. Glucose in serum, up to 5.0 g/l, was continuously determined at a rate of 60 samples per hour. The co-immobilized enzyme column gave better sensitivity as compared with an enzyme column which contained a mixture of two kinds of individually immobilized enzymes. The enzyme column was sufficiently stable while in use for two months. The results correlated satisfactorily well with those obtained by other well established methods for glucose assay.

Blood Glucose↗

1-Methylcyclopropene interactions with diphenylamine on diphenylamine degradation, alpha-farnesene and conjugated trienol concentrations, and polyphenol oxidase and peroxidase activities in apple fruit.

1-Methylcyclopropene (1-MCP) is a new technology that is applied commercially to inhibit ethylene action in apple fruit, but its interactions with existing technologies such as diphenylamine (DPA) for control of superficial scald development in fruit during and after storage is unknown. To investigate possible interactions between 1-MCP and DPA, Delicious apples were untreated or treated with 2 g L(-1) DPA, and then with or without 1 microL L(-1) 1-MCP. Ethylene production and respiration rates of fruit were measured immediately following treatment, and fruit was stored at 0.5 degrees C for 12 weeks. Internal ethylene concentrations (IEC), alpha-farnesene and conjugated trienol (CTol) concentrations, activities of peroxidase and polyphenol oxidase (PPO), and DPA levels in the skin of the fruit were measured at intervals during storage. 1-MCP reduced the rate of DPA loss from peel tissue so that by 12 weeks of storage concentrations of the chemical were 25% higher than in untreated fruit. 1-MCP, with and without DPA, markedly inhibited ethylene production and respiration rates, maintained low IEC and alpha-farnesene and CTol concentrations, while DPA had little effect on these factors except inhibition of CTol accumulation. Treatment effects on peroxidase and PPO activities were inconsistent.

Catechol Oxidase↗

Competing peroxidase and oxidase reactions in scopoletin-dependent H2O2-initiated oxidation of NADH by horseradish peroxidase.

Addition of NADH inhibited the peroxidative loss of scopoletin in presence of horseradish peroxidase and H2O2 and decreased the ratio of scopoletin (consumed):H2O2 (added). Concomitantly NADH was oxidized and oxygen was consumed with a stoichiometry of NADH:O2 of 2:1. On step-wise addition of a small concentration of H2O2 a high rate of NADH oxidation was obtained for a progressively decreasing time period followed by termination of the reaction with NADH:H2O2 ratio decreasing from about 40 to 10. The rate of NADH oxidation increased linearly with increase in scopoletin concentration. Other phenolic compounds including p-coumarate also supported this reaction to a variable degree. A 418-nm absorbing compound accumulated during oxidation of NADH. The effectiveness of a small concentration of H2O2 in supporting NADH oxidation increased in presence of SOD and decreased in presence of cytochrome c, but the reaction terminated even in their presence. The results indicate that the peroxidase is not continuously generating H2O2 during scopoletin-mediated NADH oxidation and that both peroxidase and oxidase reactions occur simultaneously competing for an active form of the enzyme.

Cytochrome c Group↗

The isozymic similarity of indoleacetic Acid oxidase to peroxidase in birch and horseradish.

The relationship of indoleacetic acid oxidase activity to peroxidase activity is complicated by numerous multiple forms of this enzyme system. It is not known if all isozymes of this complex system contain both types of activity. Isozyme analysis of commercial horseradish peroxidase and leaf extracts of yellow birch (Betula alleghaniensis) by isoelectric focusing in polyacrylamide gels was used to examine this problem. Horseradish and birch exhibited 20 and 13 peroxidase isozymes, respectively, by staining with benzidine or scopoletin. Guaiacol was less sensitive. Indoleacetic acid oxidase staining (dimethylaminocinnamaldehyde) generally showed fewer bands, and left doubt as to the residence of both types of activity on all isozymes. Elution of the isozymes from the gels and wet assays verified that all peroxidase isozymes contained indoleacetic acid oxidase activity as well. Estimation of oxidase to peroxidase ratios for the major bands indicated small differences in this parameter. A unique isozyme for one or the other type of activity was not found.

Journal Article↗

Comparison of content in phenolic compounds, polyphenol oxidase, and peroxidase in grains of fifty sorghum varieties from burkina faso.

Analysis of fifty sorghum [Sorghum bicolor (L.) Moench] varieties used in Burkina Faso showed that they have different contents of phenolic compounds, peroxidase (POX), and polyphenol oxidase (PPO). Most of the varieties (82%) had a tannin content less than 0.25% (w/w). POX specific activity was higher than the monophenolase and o-diphenolase specific activities of PPO. For POX, there was a diversity of isoforms among varieties. No clear correlation could be made between the quantitative composition of the grain in phenolics, PPO, and POX, and resistance of plant to pathogens. In general, varieties good for a thick porridge preparation ("tô") had low phenolic compounds content and a medium POX activity. From the red varieties, those used for local beer ("dolo") had a high content in phenolic compounds and PPO, and a low POX activity. The variety considered good for couscous had a low POX content. The characteristics might be useful as selection markers for breeding for specific applications.

Burkina Faso↗