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At least 1,189 records · Page 66Linked to original sources
PubMed1988

Peroxidase activity in traumatic skin lesions.

Peroxidase activity was determined in experimental compression-excoriation lesions and incision wounds of rat skin after different periods of vital time. The peroxidase enzyme was extracted from the tissues by homogenization in 0.5% cetyltrimethylammoniumbromide, and the enzyme activity was measured from the supernatant by o-dianisidine-H2O2 assay. In the blood of the rats a mean activity of approx. 5.26 +/- 1.11 U/g dry weight was observed. In the control specimens of the skin the activity was very low and generally below the detection limit of the methods used. In 30-min-old compression-excoriation lesions the mean peroxidase activity was 0.38 +/- 0.21 U/g dry weight. In lesions older than 30 min the activity started to increase rapidly. In 4-h-old compression-excoriation lesions it was 10 times higher than the 30-min level and was 40 times higher in 12-h-old lesions and 70-100 times higher in 1-3-day-old compression-excoriation lesions, respectively. In 30-min-old incision wounds the mean peroxidase activity was 0.65 +/- 0.37 U/g dry weight. The increase of the activity compared with the 30-min level was even faster in the incision wounds: in 4-h-old wounds the mean activity was 50 times higher, in 12-h-old wounds 200 times higher and in those of 1-5 days it was several hundreds of times higher. Compression-excoriation lesions made after death showed activity similar to the control specimens. Postmortem autolysis at +22 degrees C resulted in a loss of the enzyme activity in 1-day-old compression-excoriation lesions so that after 3 days approx. 80% remained, and after 5 and 7 days approx. 40% was present. After 3 days of autolysis at +4 degrees C, nearly 100% of the activity remained and approx. 90% was present after 5 and 7 days of autolysis. Increased peroxidase activity was also detectable in human vital excoriations in the specimens which were taken in autopsies several days postmortem.

Animals↗
PubMed1995

An ultrastructural study of cuneocerebellar neurons and primary afferent terminals in the external cuneate nucleus of gerbils as revealed by retrograde and transganglionic transport of horseradish peroxidase.

The present study examined the synaptic organization of cuneocerebellar neurons and their relationships with the primary afferents in the gerbil external cuneate nucleus following multiple injections of horseradish peroxidase over a widespread area in the cerebellum in conjunction with a simultaneous injection of horseradish peroxidase into the cervical or brachial nerve plexus. The external cuneate nucleus is topographically organized: the rostral portion receiving the primary afferents from the cervical plexus and the caudal portion primary afferents from the brachial plexus. This study attempted to correlate the synaptology with the topography and different cytoarchitecture in these two specific regions in the external cuneate nucleus. Ultrastructurally, the profiles of horseradish peroxidase-labelled cuneocerebellar neurons could be divided into three types, namely, small, medium and large on the basis of their cross-sectional areas. Axon terminals which formed axosomatic synapses could be classified into: round (Rs type; 22.2%), pleomorphic (Ps type; 55.6%) and flattened (Fs type; 22.2%) vesicle boutons. The horseradish peroxidase-labelled dendritic elements of the cuneocerebellar neurons were postsynaptic to a greater number of axon terminals which were also classified into Rd (77.5%), Pd (18.8%) and Fd (3.7%) type boutons. Some of the Rd boutons making direct synaptic contacts with the cuneocerebellar neurons originated from primary afferents since they were simultaneously labelled by transganglionic transport of horseradish peroxidase. In the rostral external cuneate nucleus, synapses on cuneocerebellar neurons were more frequent on their primary dendrites as compared with those on the primary dendrites of the caudal cuneocerebellar neurons. The latter, on the other hand, showed more synapses on their distal dendrites. This may have functional implications with regard to the afferent inputs to cuneocerebellar neurons in the rostral and caudal external cuneate nucleus.

Animals↗
PubMed2003

Screening of tetrachlorodibenzo- p-dioxin-degrading fungi capable of producing extracellular peroxidases under various conditions.

Forty-six pulp-bleaching fungi were screened for production of key enzymes for conversion of polychlorinated dibenzo-p-dioxins--lignin peroxidase (LiP), manganese peroxidase (MnP), and manganese-independent peroxidase (MiP)--under various conditions that would allow their utilization in the environment. Of 38 MnP-producing strains with MiP activity, 22 produced LiP. Three of the new isolates, Bjerkandera sp. strains MS191, MS325, and MS1167, were the best producers of the three different peroxidases, and had reasonable growth rates. The most promising Bjerkandera sp. strain, MS325, exhibited significant levels of LiP and MnP activities under various conditions, e.g., nutrient nitrogen-sufficient or -limited conditions, conditions with or without Mn(II), and changes in temperature (15-37 degrees C). Furthermore, the ability of this strain to degrade 1,3,6,8-tetrachlorodibenzo- p-dioxin was confirmed. The results presented here indicate that utilization of Bjerkandera sp. strain MS325 on a practical scale in the environment has several advantages over many white rot fungi, which produce extracellular peroxidases only under specific conditions such as nutrient limitation.

Azure Stains↗
PubMed2005

Peroxidases have more functions than a Swiss army knife.

Plant peroxidases (class III peroxidases) are present in all land plants. They are members of a large multigenic family. Probably due to this high number of isoforms, and to a very heterogeneous regulation of their expression, plant peroxidases are involved in a broad range of physiological processes all along the plant life cycle. Due to two possible catalytic cycles, peroxidative and hydroxylic, peroxidases can generate reactive oxygen species (ROS) (*OH, HOO*), polymerise cell wall compounds, and regulate H2O2 levels. By modulating their activity and expression following internal and external stimuli, peroxidases are prevalent at every stage of plant growth, including the demands that the plant meets in stressful conditions. These multifunctional enzymes can build a rigid wall or produce ROS to make it more flexible; they can prevent biological and chemical attacks by raising physical barriers or by counterattacking with a large production of ROS; they can be involved in a more peaceful symbiosis. They are finally present from the first hours of a plant's life until its last moments. Although some functions look paradoxical, the whole process is probably regulated by a fine-tuning that has yet to be elucidated. This review will discuss the factors that can influence this delicate balance.

Gene Expression Regulation, Plant↗
PubMed2007

An investigation of the peroxidase activity of Vitreoscilla hemoglobin.

In order to investigate the ability of the Vitreoscilla hemoglobin (VHb) to act as a peroxidase, the protein was overexpressed in Escerichia coli and purified using a 6xHis-tag. The peroxidase activity of VHb was studied using 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), ferrocene carboxylic acid (FcCOOH) dopamine and L-dopa as substrates. The effects of external agents such as pH, salt concentration/ionic strength, and the thermal stability of VHb on the catalytic activity were assessed. The optimum pH for VHb using ABTS as a substrate was estimated to be 6-7. The VHb protein proved to be stable up to 80 degrees C, as judged by its peroxidase activity. Furthermore, NaCl concentrations up to 100 mM did not exert any significant effect on the activity. The catalytic activity against ABTS and FcCOOH was similar to that measured for horseradish peroxidase, whereas in the case of the phenolic substrates dopamine and L-dopa the activity was several orders of magnitude lower. The Michaelis constants, KmH2O2, were in good agreement with the data for human and bovine hemoglobin. No activity could be detected for the negative controls lacking VHb. These results demonstrate that VHb exhibits peroxidase activity, a finding in line with the hypothesis that VHb has cellular functions beyond the role as an oxygen carrier.

Bacterial Proteins↗
PubMed2001

Buffer-anion-dependent Ca2+ leaching from horseradish peroxidase at low pH.

Despite highly conserved active-site structures, members of the plant peroxidase superfamily exhibit a wide range of pH optima. Horseradish peroxidase isozyme C (HRPC) is an ideal peroxidase to investigate the structural determinants of pH stability and activity in superfamily members. Conflicting reports exist on the low-pH stability of HRPC and consequently the pKa of the catalytic distal histidine, which is neutral in active peroxidases. Towards resolving such discrepancies, acid-induced changes in HRPC from two popular commercial suppliers were systematically analyzed. Specifically, FTIR v(CO) and Soret-CD spectra of HRPC-CO and Soret absorption of ferric HRPC were recorded to probe time-dependent heme-pocket changes at pH 3.0 in phosphate, citrate and formate buffers, while the FTIR amide I' and far-UV CD spectra were examined to probe changes in secondary structure. Both HRPC-CO samples exhibited identical pH 7.0 v(CO) bands at 1934 and 1905 cm-1. In the pH 3.0 spectrum of sample A, the 1934 cm-1 band was dominant while a broad 1969 cm-1 band appeared in sample B. The intensity of this band, which is assigned to solvent-exposed heme, was greater in citrate than phosphate buffer, but in formate the 1934 cm-1 band remained dominant. Other spectral changes mirrored the v(CO) trends. No time- or buffer-anion-dependent conformation changes were detected in 1 mM CaCl2, revealing that buffer-anion-dependent leaching of stabilizing Ca2+ from HRPC occurs at pH 3.0. Since the N-glycans present in HRPC are of the flexible protein-surface-shielding type, the variation in low-pH conformational stability of the HRPC samples could be attributed to heterogeneous glycosylation, which was detected by SDS-PAGE. It is further proposed that glycosylation patterns may affect the low-pH stability of class II and III plant peroxidases.

Anions↗
PubMed2000

Archaeal promoter-directed expression of the Halobacterium salinarum catalase-peroxidase gene.

The Halobacterium salinarum catalase-peroxidase gene was subcloned into shuttle vectors pWL102 and pWL202 and expressed under the control of different archaeal promoters. When Hbt. salinarum was transformed with the catalase-peroxidase gene under the control of its own promoter, catalase-peroxidase activity increased twofold. Catalase-peroxidase activity increased threefold when Hbt. salinarum was transformed with the catalase-peroxidase gene under the control of a tRNA promoter. This bifunctional enzyme in Hbt. salinarum was not induced by environmental stresses such as H2O2, intense light, darkness, high temperature, low temperature, redox inhibitors, heavy metals, or ions.

Base Sequence↗
PubMed1991

Heterologous expression and characterization of an active lignin peroxidase from Phanerochaete chrysosporium using recombinant baculovirus.

The cDNA clone lambda ML-1 encoding one of the extracellular lignin peroxidases from the white rot fungus, Phanerochaete chrysosporium, was heterologously expressed in an active form using a recombinant baculovirus system. The glycosylated extracellular form of the recombinant protein contained the ferriprotoporphyrin IX moiety and was capable of oxidizing both iodide and the model lignin compound, veratryl alcohol. In comparative peroxidase assays using guaiacol and Mn(II), the recombinant lignin peroxidase did not appear to be Mn(II) dependent. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis demonstrated that the heterologously expressed peroxidase had an apparent molecular weight similar to that of the native fungal isozyme H8. The elution profile of the active recombinant enzyme derived by ion-exchange chromatography and immunoblot analysis using an anti-H8 monoclonal antibody provided further evidence that the lambda ML-1 DNA encodes the lignin peroxidase H8.

Baculoviridae↗
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↗
PubMed1995

Reductions catalyzed by a quinone and peroxidases from Phanerochaete chrysosporium.

A quinone produced from veratryl alcohol by lignin peroxidase from the white rot fungus Phanerochaete chrysosporium was tested for its ability to mediate reduction. The quinone (2-hydroxymethyl-5-methoxy-1,4-benzoquinone), reduced chemically or by cellobiose:quinone reductase isolated from cultures of the fungus, mediated the reduction of cytochrome c in reactions containing either Mn(III), a manganese-dependent peroxidase, Mn(II) and H2O2, or lignin peroxidase and H2O2. Formation of the semiquinone, the species responsible for reducing cytochrome c, was observed by electron spin resonance spectroscopy in these reactions. The production of the quinone was observed in the extracellular fraction of cultures grown under nutrient nitrogen-deficient conditions (2.4 mM ammonium tartrate) for over 10 days, starting on Day 2, but not under nutrient nitrogen-sufficient conditions. These results suggest that a quinone produced by lignin peroxidase can serve as a physiological mediator of reductive reactions catalyzed by the fungal peroxidases.

Benzoquinones↗
PubMed1984

The permeability of mammalian nonkeratinized oral epithelia to horseradish peroxidase applied in vivo and in vitro.

Horseradish peroxidase, an intercellular tracer, was injected sub-epithelially beneath keratinized gingiva and a variety of nonkeratinized oral epithelia. Fresh tissue biopsies from the same regions were also incubated with this tracer for 1 h. In separate experiments, horseradish peroxidase was applied topically to biopsies of oral mucosa maintained in tissue culture for periods up to 12 h. All specimens were treated so as to visualize the site of peroxidase penetration and the tissues were examined with the light and electron microscopes. In all the epithelia, a surface barrier was evident from which the tracer had been excluded. This was often narrow in the thin, nonkeratinized epithelia and could only be identified unambiguously with the electron microscope. Membrane-coating granules of the so-called nonkeratinized type were invariably associated with superficial plasma membrane of epithelial cells at the level where the barrier was first seen. The results suggest that a permeability barrier exists to horseradish peroxidase in all nonkeratinized oral epithelia with a similar location to that seen in the keratinized oral tissues. However, results obtained with a water-soluble tracer such as horseradish peroxidase may not apply to many drugs, the ready absorption of which may reflect their high lipid solubility.

Animals↗
PubMed1980

Peroxidase content of soybean root nodules.

A peroxidase has been isolated from soybean nodules and its main characteristics have been determined. Its molecular weight (48 000) and spectral properties are similar to those of usual plant peroxidases. Its activity is comparable to that of low-efficiency plant peroxidases. The rate constant of the reaction with H2O2 is 3 x 10(5) M-1 x s-1. In this reaction, nodule peroxidase yields an oxidized intermediate analogous to the compound I species of peroxidases already studied. A comparison is made with the pseudoperoxidatic activity of soybean leghemoglobin components. Leghemoglobins a and c react with H2O2 with rate constants of 5 x 10(3) and 2.5 x 10(3) M-1 x s-1, respectively, yielding the leghemoglobin (IV) species. During these reactions leghemoglobins are inactivated.

Kinetics↗
PubMed1990

Chemotactic activity for human PMN generated during ethanol metabolism by rat hepatocytes: role of glutathione and glutathione peroxidase.

Infiltration of the liver by polymorphonuclear leukocytes is a characteristic feature of alcoholic hepatitis. We have previously shown that liver cytosol metabolizing ethanol generates chemoattractant activity for polymorphonuclear leukocytes and that hydroxyl radical scavengers inhibit this process. To investigate the possibility that endogenous glutathione and glutathione peroxidase also inhibit this process, we evaluated chemoattractant activity production by glutathione and glutathione peroxidase deficient rat liver cytosol during ethanol metabolism. Incubation of cytosol deficient in both glutathione and glutathione peroxidase with 10 mM ethanol for 1 hour resulted in a 500-fold increase in chemoattractant activity when compared to cytosol with normal glutathione and glutathione peroxidase content. These findings provide further evidence for a role of oxygen free radicals in the generation of chemotactic activity and they also suggest that the ethanol-induced decrease in hepatic glutathione and glutathione peroxidase reported by others may have a significant potentiating effect on the recruitment of pro-inflammatory cells into the liver.

Animals↗
PubMed1983

Influence of estrogens on peroxidase activity in the Syrian hamster liver, kidney, and renal adenocarcinoma.

Only very low levels of peroxidase activity were detected in castrated male hamster kidneys [1.0 +/- 0.8(S.E.) units/g protein], and chronic estrogen administration, either diethylstilbestrol (DES) or 17 beta-estradiol, for 1-5 months did not result in any appreciable increase in this activity. In contrast, hamster liver peroxidase activity was initially 10- to 20-fold higher than kidney levels, and chronic estrogen treatment for similar periods resulted in up to a 9-fold elevation in the activity of this enzyme. Moreover, the level of liver peroxidase activity in both intact and in 5 alpha-dihydrotestosterone-treated castrate hamsters was 2-fold higher than castrate-untreated values. Pure renal carcinoma induced after 9 months of estrogen treatment exhibited peroxidase values similar to those found in hamster livers [124 +/- 27 (S.E.) units/g protein] following estrogen treatment. When administered concomitantly with DES, tamoxifen significantly reduced the elevated levels of liver peroxidase activity observed after 2 months of DES treatment alone. A high affinity (KA = 0.10 X 10(9)M-1) estrogen receptor was found in liver cytosols of DES-treated hamsters which had increased slightly from untreated castrate levels.

Adenocarcinoma↗
PubMed1988

Kinetic mechanism and substrate specificity of glutathione peroxidase activity of ebselen (PZ51).

The glutathione peroxidase activity of ebselen (PZ51) was studied using different hydroperoxidic substrates. The single progression curves obtained in the spectrophotometric test were processed by a computer to fit the integrated rate equation that describes the ping pong reaction of the Se glutathione peroxidase. Ebselen catalyzes the GSH peroxidase reaction with a mechanism that appears kinetically identical to the mechanism of the enzymes. The inactivation of the catalytic properties of ebselen by iodoacetate suggests that a selenol moiety is involved. Among the substrates tested, the best hydroperoxidic substrates are the hydroperoxy derivatives of phosphatidyl choline. Ebselen is active also on membrane hydroperoxides as does phospholipid hydroperoxide glutathione peroxidase but not glutathione peroxidase.

Antioxidants↗
PubMed1989

Glutathione S-transferases and glutathione peroxidases in doxorubicin-resistant murine leukemic P388 cells.

Energy-dependent rapid drug efflux is believed to be a major factor in cellular resistance to doxorubicin (DOX). However, several recent studies have demonstrated that cellular DOX retention alone does not always correlate with its cytotoxicity and suggest that mechanisms other than rapid drug efflux may also be important. In the present study, we have compared glutathione (GSH) S-transferase (GST), selenium-dependent GSH peroxidase and selenium-independent GSH peroxidase II activities in DOX-sensitive (P388/S) and resistant (P388/R) mouse leukemic cells. The GST activity towards 1-chloro-2,4-dinitrobenzene (CDNB) and ethacrynic acid (EA) was markedly higher in P388/R cells compared to P388/S cells. Purification of GST by GSH-affinity chromatography from an equal number of P388/S and P388/R cells revealed an increased amount of GST protein in P388/R cells. Immunological studies indicated that alpha and pi type GST isoenzymes were 1.27- and 2.2-fold higher, respectively, in P388/R cells compared to P388/S cells. Selenium-dependent GSH peroxidase activity was similar in both the cell lines, whereas selenium-independent GSH peroxidase II activity was approximately 1.36-fold higher in P388/R cells compared to P388/S cells. These results suggest that increased GSH peroxidase II activity in P388/R cells may contribute to cellular DOX resistance by enhancing free radical detoxification in this cell line.

Animals↗
PubMed1994

The origin and composition of peroxidase-positive granules in cysteamine-treated astrocytes in culture.

Gomori astrocytes, which are prominent in periventricular regions of the brain, contain inclusions that stain with Gomori dyes, and exhibit an orange-red autofluorescence and a non-enzymatic peroxidase activity. Recently, such astrocytes have been induced in dispersed glial cultures by exposure to cysteamine. Using these cells, we have shown that the peroxidase-positive inclusions (Gomori bodies) are multicompartmental, that iron co-localizes with the peroxidase activity, and that the iron is often segregated in one of the compartments of the body. The goal of the present study was to determine the origin and process of formation of these bodies. The results indicate that cysteamine induces aberrations in mitochondrial structure associated with the acquisition of iron and the associated peroxidase activity. Mitochondria thus transformed appear to initiate an autophagic process in which they, and adjacent structures, are sequestered. The presence of acid phosphatase activity in a number of mature Gomori bodies attests to the participation of lysosomal elements in this process. These results indicate, therefore, that the Gomori body is a complex autophagosome in which the iron-containing compartments, putatively responsible for the peroxidase activity, represent undegraded transformed mitochondria.

Acid Phosphatase↗
PubMed1983

Diaminobenzidine peroxidase in rat brain.

Peroxidase has several roles in each organ. In neural tissue, it is considered from pathological examination to be related to the aging process. To study biochemically the presence of peroxidase, diaminobenzidine was used as the hydrogen donor and the enzyme was partially purified from rat brain and characterized. Diaminobenzidine peroxidase was purified 670-fold from the original homogenate. The presence of p-phenylenediamine and guaiacol peroxidase was not detected in either the crude homogenate or the partially purified fraction. The possible presence of isozyme(s) in peroxidase was implied and this may be related to the physiologic differences in organs.

Animals↗