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PubMed1994

Pyranose Oxidase, a Major Source of H(2)O(2) during Wood Degradation by Phanerochaete chrysosporium, Trametes versicolor, and Oudemansiella mucida.

The production of the H(2)O(2)-generating enzyme pyranose oxidase (POD) (EC 1.1.3.10) (synonym, glucose 2-oxidase), two ligninolytic peroxidases, and laccase in wood decayed by three white rot fungi was investigated by correlated biochemical, immunological, and transmission electron microscopic techniques. Enzyme activities were assayed in extracts from decayed birch wood blocks obtained by a novel extraction procedure. With the coupled peroxidase-chromogen (3-dimethylaminobenzoic acid plus 3-methyl-2-benzothiazolinone hydrazone hydrochloride) spectrophotometric assay, the highest POD activities were detected in wood blocks degraded for 4 months and were for Phanerochaete chrysosporium (149 mU g [dry weight] of decayed wood), Trametes versicolor (45 mU g), and Oudemansiella mucida (1.2 mU g), corresponding to wood dry weight losses of 74, 58, and 13%, respectively. Mn-dependent peroxidase activities in the same extracts were comparable to those of POD, while lignin peroxidase activity was below the detection limit for all fungi with the veratryl alcohol assay. Laccase activity was high with T. versicolor (422 mU g after 4 months), in trace levels with O. mucida, and undetectable in P. chrysosporium extracts. Evidence for C-2 specificity of POD was shown by thin-layer chromatography detection of 2-keto-d-glucose as the reaction product. By transmission electron microscopy-immunocytochemistry, POD was found to be preferentially localized in the hyphal periplasmic space of P. chrysosporium and O. mucida and associated with membranous materials in hyphae growing within the cell lumina or cell walls of partially and highly degraded birch fibers. An extracellular distribution of POD associated with slime coating wood cell walls was also noted. The periplasmic distribution in hyphae and extracellular location of POD are consistent with the reported ultrastructural distribution of H(2)O(2)-dependent Mn-dependent peroxidases. This fact and the dominant presence of POD and Mn-dependent peroxidase in extracts from degraded wood suggest a cooperative role of the two enzymes during white rot decay by the test fungi.

Journal Article↗
PubMed1995

Lignin Peroxidases, Manganese Peroxidases, and Other Ligninolytic Enzymes Produced by Phlebia radiata during Solid-State Fermentation of Wheat Straw.

The white rot fungus Phlebia radiata 79 (ATCC 64658) produces lignin peroxidase (LiP), manganese peroxidase (MnP), glyoxal oxidase (GLOX), and laccase in the commonly used glucose low-nitrogen liquid medium. However, the enzymes which this fungus utilizes for selective removal of lignin during degradation of different lignocellulosic substrates have not been studied before. Multiple forms of LiP, MnP, GLOX, and laccase were purified from P. radiata culture extracts obtained after solid-state fermentation of wheat straw. However, the patterns of extracellular lignin-modifying enzymes studied were different from those of the enzymes usually found in liquid cultures of P. radiata. Three LiP isoforms were purified. The major LiP isoform from solid-state cultivation was LiP2. LiP3, which has usually been described as the major isoenzyme in liquid cultures, was not expressed during straw fermentation. New MnP isoforms have been detected in addition to the previously reported MnPs. GLOX was secreted in rather high amounts simultaneously with LiP during the first 2 weeks of growth. GLOX purified from P. radiata showed multiple forms, with pIs ranging from 4.0 to 4.6 and with a molecular mass of ca. 68 kDa.

Journal Article↗
PubMed2004

Physiology and nutrition of Treponema primitia, an H2/CO2-acetogenic spirochete from termite hindguts.

Treponema primitia strains ZAS-1 and ZAS-2, the first spirochetes to be isolated from termite hindguts (J. R. Leadbetter, T. M. Schmidt, J. R. Graber, and J. A. Breznak, Science 283:686-689, 1999), were examined for nutritional, physiological, and biochemical properties relevant to growth and survival in their natural habitat. In addition to using H(2) plus CO(2) as substrates, these strains were capable of homoacetogenic growth on mono- and disaccharides and (in the case of ZAS-2) methoxylated benzenoids. Cells were also capable of mixotrophic growth (i.e., simultaneous utilization of H(2) and organic substrates). Cell extracts of T. primitia possessed enzyme activities of the Wood/Ljungdahl (acetyl coenzyme A) pathway of acetogenesis, including tetrahydrofolate-dependent enzymes of the methyl group-forming branch. However, a folate compound was required in the medium for growth. ZAS-1 and ZAS-2 growing on H(2) plus CO(2) displayed H(2) thresholds of 650 and 490 ppmv, respectively. Anoxic cultures of ZAS-1 and ZAS-2 maintained growth after the addition of as much as 0.5% (vol/vol) O(2) to the headspace atmosphere. Cell extracts exhibited NADH and NADPH peroxidase and NADH oxidase activities but neither catalase nor superoxide dismutase activity. Results indicate that (i) T. primitia is able to exploit a variety of substrates derived from the food of its termite hosts and in so doing contributes to termite nutrition via acetogenesis, (ii) in situ growth of T. primitia is likely dependent on secretion of a folate compound(s) by other members of the gut microbiota, and (iii) cells possess enzymatic adaptations to oxidative stress, which is likely to be encountered in peripheral regions of the termite hindgut.

Acetic Acid↗
PubMed1973

Fractionation of dipeptidase activities of Streptococcus lactis and dipeptidase specificity of some lactic acid bacteria.

Proteins in sonic extracts of Streptococcus lactis were separated by starch-gel electrophoresis at high voltage. Each slab was sliced longitudinally, and half was stained for peptidases in a mixture containing a peptide, L-amino acid oxidase (snake venom), peroxidase, and o-dianisdine; the other half was stained in amido black for protein. In addition to sonic treatment, trypsin also released enzyme from acetone-treated cells. Glycyl-L-phenylalanine, L-phenylalanyl-glycine, L-alanyl-L-phenylalanine, and L-phenylalanyl-L-alanine served as substrates in characterizing the enzymes. Five different fractions of various specificities appeared in the gels. Broad-range substrate specificities were found for sonic extracts of S. lactis, S. cremoris, S. durans, and Lactobacillus acidophilus.

Alanine↗
PubMed1984

Effect of type A Pasteurella multocida fractions on bovine polymorphonuclear leukocyte functions.

The effect of various Pasteurella multocida fractions on bovine polymorphonuclear leukocyte (PMN) functions was examined in vitro by using two encapsulated strains, P-2383 and P-1062 (both are Carter capsular type A and of bovine origin). The ability of PMNs to ingest Staphylococcus aureus and iodinate protein was significantly inhibited in the presence of live cells, heat-killed whole cells, or saline-extracted capsules but not in the presence of the decapsulated heat-killed cells. None of the fractions of the two strains inhibited nitroblue tetrazolium reduction by PMNs. The saline extract did not inhibit the binding of iodine to protein by a reaction involving xanthine, xanthine oxidase, and horseradish peroxidase. The PMN inhibitory factor was further characterized as a heat-stable capsular material of greater than 300,000 molecular weight.

Animals↗
PubMed1993

Morphology and topography of identified primary afferents in trigeminal subnuclei principalis and oralis.

1. Intra-axonal recording, receptive field mapping, horseradish peroxidase injection, cytochrome oxidase staining, and computer-assisted reconstruction/morphometric methods were used to elucidate the structure and topography of trigeminal primary afferent collaterals in the normal adult rat. Prior studies focused on trigeminal brain stem subnuclei interpolaris and caudalis. This work is extended here to the remaining 2 subnuclei, principalis (PrV) and oralis (SpVo), where collaterals from 66 axons in 37 adult rats were studied. In nine rats, three to five axons were stained for within-nucleus comparisons of different fibers. Quantitative analyses were restricted to vibrissa sensitive fibers. 2. All of the axons conducted rapidly with small, low-threshold receptive fields. The majority responded to vibrissa deflection (n = 47); the remainder responded to guard hair deflection; gentle pressure applied to hairy skin, glabrous skin, lingual mucosa, or an incisor; or jaw movement. All descended in the trigeminal sensory root where some bifurcated into ascending and descending branches. Each well-stained fiber gave rise to transversely oriented collaterals in PrV and SpVo. 3. Within PrV and SpVo, fibers with differing adaptation properties and receptive fields had indistinguishable collateral morphologies. Arbors from single axons were rostrocaudally discontinuous, small relative to collaterals in subnuclei interpolaris and caudalis, circumscribed and topographically organized in a manner consistent with cytochrome oxidase and bulk-labeled primary afferent staining patterns. In SpVo and caudal PrV, the map is inverted with the nose pointing medially. In rostral PrV, the map turns 90 degrees such that the nose points dorsally. 4. Axons had different quantitative properties along the rostrocaudal axis of the trigeminal brain stem complex. Whereas arbors subtended similar transverse areas throughout PrV and SpVo, collaterals in the rostral third of PrV had a relatively low bouton density. Arbors in the caudal two thirds of PrV had the highest bouton density. Arbors in SpVo tended to be more variable in size and shape than those of caudal PrV, and their bouton numbers were significantly lower than in PrV. 5. In PrV, arbors were largely confined to somatotopically corresponding cytochrome oxidase patches, precluding significant overlap of neighboring whisker projections. In SpVo, termination sites were not as strictly confined and numerous examples of within- and between-row overlap were obtained for whisker afferents in cases where multiple axons were stained.(ABSTRACT TRUNCATED AT 400 WORDS)

Afferent Pathways↗
PubMedDate not supplied

[Monitoring of adipocyte responsiveness by in situ microdialysis in lipodystrophy tissue: adjustment of a glycerol quantification method in small samples].

In situ microdialysis allows monitoring of metabolic cellular processes at the tissue level in vivo. In the assessment of physiopathologic alterations seen in lipodystrophy, monitoring of glycerol release is pivotal. Indeed, it allows to quantify the pharmacological responsiveness of subcutaneous adipose tissue in humans. Until now, the small volume of microdialysate collected (5-15 microL/sample) restricted the assessment of glycerol level to the use of the radio-enzymatic method or the reference spectrophotometric microanalysis technique. The aim of this study was to adapt the method of glycerol measurement by iminequinone spectrophotometry colorimetric assay (520 nm) using the following reagent: 0.5 IU Glycerokinase, 1.23 IU glycerophosphate oxidase, 0.98 IU peroxidase, 4.6 mM Mg, 5.4 mM 4-chlorophenol, 0.25 mM 4-aminoantipyrine and 1.4 mM ATP. The assay was setup to run on Olympus AU 2700 automate (15 pL sample volume). The sensitivity of the method was improved by adding a 0.2 mmol triglyceride (TG) solution and 1.5 IU lipase to samples, reducing the limit of free glycerol quantification to 0.020 mmol/L. The analytical repeatability was 2.0% and the reproducibility was 7.9%. The present method thus demonstrated the feasibility of pharmacodynamic exploration of local cutaneous responsiveness in vivo in clinical trials.

Adipocytes↗
PubMed2003

[Real-time detection of neurotransmitter release and its spatial distribution].

Neurotransmitters have been well known as information carriers for a long time. Recently, some of the research indicated their neurotoxicity, while some indicated their neurotrophic actions. It is very important to understand the role of neurotransmitters. Glutamate is one of the most important excitatory neurotransmitter in the brain. We developed a novel measurement method for glutamate. The method we describe here is based on the enzyme-mediated electrochemical detection. Glutamate oxidase and horseradish peroxidase were deposited together with polymer-mediator on the electrode. We applied this idea on ITO multi-array electrode and developed a 64 channel multi-array sensor. The sensor permits us to detect glutamate release from multiple regions simultaneously in real time. As it is possible to illustrate the distribution of glutamate release, the sensor could be used not only in the pharmacological field, but also in medical treatment in the near future.

Animals↗
PubMed2002

Biosynthesis of p-anisaldehyde by the white-rot basidiomycete Pleurotus ostreatus.

The white-rot basidiomycete Pleurotus ostreatus produced sweet flavor compounds on a liquid medium. The major and minor compounds identified by GC-MS analysis were p-anisaldehyde (4-methoxybenzaldehyde) and 3-chloro-p-anisaldehyde (3-chloro-4-methoxybenzaldehyde), respectively. p-Anisaldehyde was only produced under static culture conditions. Differences in the type and quantity of flavor compounds produced among wild strains of P. ostreatus were observed. Aryl alcohol oxidase and manganese peroxidase activities increased parallel to the production of p-anisaldehyde. These results indicated that the biosynthesis of p-anisaldehyde is concerned in generating H2O2-activated peroxidase in the lignin-degradation system. Addition of L-tyrosine to the culture led to higher production of p-anisaldehyde. The flavor extract, which contains p-anisaldehyde, exhibited antimicrobial activity against Bacillus subtilis, Pseudomonas aeruginosa, Aspergillus niger and Fusarium oxysporum.

Journal Article↗
PubMed1986

Evaluation of the spectrophotometric assay of guanase with 2,2'-azino-di(3-ethylbenzthiazoline-6-sulphonate) (ABTS) as chromogen.

A simple spectrophotometric assay for serum guanase based on the oxidation of 2,2'-azino-di(3-ethylbenzthiazoline-6-sulphate) (ABTS) using xanthine oxidase, uricase and peroxidase is described and statistically examined through its application to normal and pathological sera. The method is very sensitive, precise (CV below 8.13%) and linear up to 152.5 U/l. Comparison with the methods of Hue & Free ((1965) Clin. Chem. 11, 708-715), and Giusti ((1974) In: Methods of Enzymatic Analysis, Bergmeyer, H. U., ed., p. 1086), and Ito et al. ((1981) Clin. Chim. Acta 115, 135-144) gave a good correlation (r greater than or equal to 0.969). The reference values for the ABTS-method are 2.93 to 23.92 U/l (mean = 13.57 U/l, CV = 22.43%). The mean values of guanase activities determined in sera of patients with different liver diseases (mean = 30.29 U/l), or chronic alcoholics (mean = 35.41 U/l) were significantly higher than normal. The patients with chronic diseases had significantly lower activity (mean = 7.22 U/l, t = 9.25, p less than 0.001).

Alcoholism↗
PubMed2003

Simultaneous determination of choline and acetylcholine based on a trienzyme chemiluminometric biosensor in a single line flow injection system.

A detector for the simultaneous determination of choline (Ch) and acetylcholine (ACh) based on a sensitive trienzyme chemiluminometric biosensor in a single line flow injection (FI) system is described. Immobilized choline oxidase (ChOx), immobilized peroxidase (POx), immobilized acetylcholinesterase, and coimmobilized ChOx/POx were packed, in turn, in a transparent ETFE tube (1 mm i.d., 75 cm) and the tube was placed in front of a photomultipier tube as a flow cell. Two-peak response was obtained by one injection of the sample solution. The first and second peaks were dependent on the concentrations of Ch and ACh, respectively. The influence of some experimental parameters such as flow rate, amounts of immobilized enzymes on the behavior of the sensor was studied in order to optimize the sensitivity, sample throughput and resolution. Calibration curves were linear at 1 - 1000 nM for Ch and 3 - 3000 nM for ACh. The sample throughput was 25/h without carryover. The FI system was applied to the simultaneous determination of Ch and ACh in rabbit brain tissue homogenates.

Acetylcholine↗
PubMed2005

Production and degradation of oxygen metabolites during inflammatory states in the human lung.

Lung represents a tissue that encounters a high oxidant burden but is also endowed with efficient protection against oxygen and reactive oxygen species (ROS). The oxidant stress experienced by the lung is enhanced by exogenous oxidant producing toxins most importantly pollutants and cigarette smoke, as well as by increased oxidant production during lung inflammation. The major oxidant generating enzymes present in human lung include NADPH oxidase, myeloperoxidase, eosinophil peroxidase and nitric oxide synthases, all of which are induced during inflammatory states. The antioxidant machinery of human lung against ROS is more versatile than often assumed. In addition to metal binding proteins, mucus components and small molecular weight antioxidants and vitamins, lung tissue possesses a highly cell specific and compartmentalized defense system containing several antioxidant enzymes with variable locations, inducibilities and kinetics. Inflammatory states like asthma, chronic obstructive lung disease (COPD) and parenchymal lung disorders have been shown to lead to serious disturbances in the oxidant/antioxidant balance of the lung with consequent oxidant mediated cell injury. Novel synthetic antioxidant mimetics may have the potential to slow or terminate the progression of lung diseases associated with free radicals.

Animals↗
PubMed2004

The role of oxygen in the viability of probiotic bacteria with reference to L. acidophilus and Bifidobacterium spp.

The various therapeutic benefits of Lactobacillus acidophilus and Bifidobacterium spp. have resulted in their increased incorporation into dairy foods such as yoghurts. Currently however, the efficacy of these probiotic bacteria is limited by their poor survival during the shelf life of yoghurt. Oxygen toxicity is widely considered to be responsible for the cell deaths of these bacteria. The intestinal origins and the microaerophilic and anaerobic characteristics of L. acidophilus and Bifidobacterium spp. respectively, can render them susceptible to oxygen contained in the food products. This review discusses the influence of the dissolved oxygen in yogurt on the viability of these bacteria. Suggested techniques to protect these probiotic bacteria from oxygen toxicity are evaluated. Although the problem of oxygen toxicity in probiotic bacteria is regarded as significant, little is known however about the cellular interaction of these bacteria with oxygen. This review summarizes what is known about the biochemistry of oxygen toxicity in these bacteria. The various metabolic and biochemical responses of L. acidophilus and Bifidobacterium to oxygen are examined. Additionally, the importance of NADH oxidase and NADH peroxidase in the oxygen tolerance of these bacteria is evaluated and assays used to measure their cellular concentrations are discussed.

Bifidobacterium↗
PubMed1989

Rapid enzymatic determination of urinary oxalate.

This new reagent kit for the quantitative measurement of oxalate in urine is a modification of an earlier Sigma oxalate assay procedure (procedure no. 590), a coupled enzyme assay involving oxalate oxidase and horseradish peroxidase. The new analytical procedure includes methods for processing urine specimens to eliminate interference with oxalate color development at 590 nm by ascorbic acid, divalent cations, and other urinary constituents. The reaction is complete in less than 5 min, and results are linearly related to oxalate concentration up to at least 1 mmol/L. Assay sensitivity and within-run and between-run precision were within the limits acceptable for other urinary oxalate procedures. Analytical recovery of added oxalate was close to 100%. This specific, simple, rapid procedure is suitable for routine clinical use.

Ascorbic Acid↗
PubMed1988

An enzymatic method for erythrocyte acetylcholinesterase.

The acetylcholinesterase (EC 3.1.1.7) in 50 microL of a 61-fold dilution of erythrocytes in water hydrolyzes acetylcholine during a timed 20-min reaction at 37 degrees C. The resulting choline is measured by use of choline oxidase coupled to peroxidase, with phenol and aminoantipyrene to give a pink product that absorbs maximally at 500 nm. For calibration, a choline iodide standard is included in each batch of up to 19 samples. Accuracy was assessed by using specific inhibitors and measuring choline in the presence of excess erythrocyte solution. The standard curve for the assay is linear to threefold the normal enzyme activity. Between-batch precision was 0.40 kU/L at a mean of 11.5 kU/L (CV 3.5%), and comparison with an acetylthiocholine procedure (x) gave a good correlation: y = 1.02x - 0.27 kU/L (r = 0.991). Long-term precision (10 months), assessed from three sets of assays of samples from 17 individuals, was 0.71 kU/L at a mean of 11.7 kU/L (CV 6.1%).

Acetylcholine↗
PubMed1986

[Current therapeutic concepts in the treatment of myocardial ischemia. Current and future drugs].

If myocardial ischemia always results from an imbalance between the needs and supplies in oxygen of the myocardium cells, the physiopathology of this process seems today infinitely more complex than the mere diminution or interruption of the output in a coronary artery. The extension of atheromatous lesions, the platelets aggregation, thrombosis, the coronary spasm, the release of products from the arachidonic cascade, the reactivity of the vascular endothelium, the profibrinolytic activity of the tissues are many of the intricate factors inducing myocardial ischemia. Cellular alterations, of which some are triggered by the release of oxygenated free radicals, lead then to an irreversible necrosis. The medications used until now in the treatment of angina are oxygen scavengers and research goes on in this direction with vaso-dilators beta-blockers, prolonged action nitro-compounds (nicorandil) or nitro-compounds with an action reinforced by N-acetyl-cysteine, bradycardiac derivates of alinidine and the new calcium antagonists dihydropyridine. However, the new physiopathological concepts of ischemia have opened new directions for the research: products which modify the arachidonic cascade by increase of synthesis or release of PGI2 (nafazatrom, defibrotide), by inhibition of TXA2 synthesis or blocking of TXA2 receptors, and similar products of PGI2 (iloprost); thrombolytic agents more specific of thrombin (PTA) or fibrinolysis activators (defibrotide), and anticoagulants with extended action; chelating agents of oxygenated free radicals (peroxide dismutase, catalase, peroxidase) or xanthine oxidase inhibitors; platelets anti-aggregates like ticlopidine which blocks the platelets receptors to fibrinogen, or inhibitors of the synthesis of pro-aggregating agents.(ABSTRACT TRUNCATED AT 250 WORDS)

Adrenergic beta-Antagonists↗
PubMed1984

A medicolegal study on enzymic fluorometry of choline in human semen.

Studies have been conducted on an enzymic fluorometric method based on an initial rate of reaction for the determination of choline. The reaction system consists of choline oxidase coupled to peroxidase and homovanillic acid. Concentrations of choline as low as 0.1 nmol could be detected by this procedure. The concentration of free choline in normal semen was 18.7 to 29.5 mumol/mL. Free choline in other body fluids was negligible. The choline concentrations in seminal stains maintained at room temperature were not changed during a 30-day period. Those concentrations in seminal fluids kept at room temperature were detected until at least the fifth day.

Alcohol Oxidoreductases↗
PubMed2006

Electrostatic environment of hemes in proteins: pK(a)s of hydroxyl ligands.

The pK(a)s of ferric aquo-heme and aquo-heme electrochemical midpoints (E(m)s) at pH 7 in sperm whale myoglobin, Aplysia myoblogin, hemoglobin I, heme oxygenase 1, horseradish peroxidase and cytochrome c oxidase were calculated with Multi-Conformation Continuum Electrostatics (MCCE). The pK(a)s span 3.3 pH units from 7.6 in heme oxygenase 1 to 10.9 in peroxidase, and the E(m)s range from -250 mV in peroxidase to 125 mV in Aplysia myoglobin. Proteins with higher in situ ferric aquo-heme pK(a)s tend to have lower E(m)s. Both changes arise from the protein stabilizing a positively charged heme. However, compared with values in solution, the protein shifts the aquo-heme E(m)s more than the pK(a)s. Thus, the protein has a larger effective dielectric constant for the protonation reaction, showing that electron and proton transfers are coupled to different conformational changes that are captured in the MCCE analysis. The calculations reveal a breakdown in the classical continuum electrostatic analysis of pairwise interactions. Comparisons with DFT calculations show that Coulomb's law overestimates the large unfavorable interactions between the ferric water-heme and positively charged groups facing the heme plane by as much as 60%. If interactions with Cu(B) in cytochrome c oxidase and Arg 38 in horseradish peroxidase are not corrected, the pK(a) calculations are in error by as much as 6 pH units. With DFT corrected interactions calculated pK(a)s and E(m)s differ from measured values by less than 1 pH unit or 35 mV, respectively. The in situ aquo-heme pK(a) is important for the function of cytochrome c oxidase since it helps to control the stoichiometry of proton uptake coupled to electron transfer [Song, Michonova-Alexova, and Gunner (2006) Biochemistry 45, 7959-7975].

Animals↗