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PubMed2000

Partial characterization of peroxidase and polyphenol oxidase activities in blackberry fruits.

A partial characterization of peroxidase (POD) and polyphenol oxidase (PPO) activities in blackberry fruits is described. Two cultivars of blackberry (Wild and Thornless) were analyzed for POD and PPO activities. Stable and highly active POD and PPO extracts were obtained using insoluble poly(vinylpyrrolidone) and Triton X-100 in 0.05 M sodium phosphate, pH 7.5, buffer. Blackberry POD and PPO activities have a pH optimum of 6.5, in a reaction mixture of 0.2 M sodium phosphate. Optimal POD activity was found with 3% o-dianisidine. Maximum PPO activity was found with catechol (catecholase activity) followed by 4-methylcatechol. Polyacrylamide gel electrophoresis of blackberry extracts under non-denaturing conditions resolved in various bands. In the POD extracts of Wild fruits, there was only one band with a mobility of 0.12. In the Thornless POD extracts there were three well-resolved bands, with R(f) values of 0.63, 0.36, and 0.09. Both the Wild and Thornless blackberry cultivars produced a single band of PPO, with R(f) values of 0.1 for Wild and 0.06 for Thornless.

Buffers↗
PubMed2003

Enzymatic browning and biochemical alterations in black spots of pineapple [Ananas comosus (L.) Merr.].

Penicillium funiculosum Thom. was consistently isolated from pineapple-infected fruitlet (black spots). Polyphenol oxidase, peroxidase, and laccase activities were determined in extracts from contiguous and infected fruitlets. Healthy fruitlets showed a rather high level of polyphenol oxidase (optimum pH 7.0), and this activity was tremendously increased (X 10) in contiguous infected fruitlets. Furthermore, infected fruitlets also exhibited laccase activity (optimum pH 4.0), while peroxidase was rather constant in both fruitlets. Browning reactions were attributed to qualitative and quantitative modifications of the enzymatic equipment (polyphenol oxidase and laccase) (p < 0.0001). In infected fruiltets, sucrose and L-malic acid were present at significantly lower amounts than in healthy ones, likely owing to fungal metabolism (p < 0.0001), whereas cell wall material was three times higher, which could be viewed as a defense mechanism to limit expansion of the mycelium.

Ananas↗
PubMed1975

Effects of titanium compounds on a D-glucose-D-glucose oxidase assay system.

Titanium compounds affect the measurement of D-glucose oxidase (and therefore D-glucose) by the D-glucose-D-glucose oxidase-peroxidase-2,2'-azinobis-(3-ethylbenzothiazoline-6-sulphonic acid) assay system. The validity of measurement of the activity of D-glucose oxidase immobilised on supports based on titanium oxides is affected by complexation of the intermediate hydrogen peroxide with the support, and such supports may prove to be unsuitable for the immobilisation of D-glucose oxidase. The formation of titanic peroxides is among the reasons discussed for the various interactions encountered. The use of the assay system for the determination of D-glucose oxidase contaminated with catalase and for the determination of hydrogen peroxide is also described.

Glucose Oxidase↗
PubMed1976

The oxidation of dithiothreitol by peroxidases and oxygen.

Horseradish peroxidase (1.11.1.7), lactoperoxidase (1.11.1.7), and the fragment of cytochrome c known as microperoxidase have been shown to catalyze the oxidation of reduced dithiothreitol in an oxygen-consuming reaction. Evidence for horseradish peroxidase intermediates compound III and compound II has been observed, although ferroperoxidase was not identified during the course of the reaction. The stoichiometry has been extablished as 1 : 1 for oxygen consumed to dithiothreitol oxidized. Cysteine and glutathione have also been shown to be substrates for horseradish peroxidase oxidase reaction.

Catalase↗
PubMed1985

Resonance Raman evidence for the activation of dioxygen in horseradish oxyperoxidase.

Resonance Raman spectroscopy has been employed to investigate the molecular bases for the markedly different properties of horseradish oxyperoxidase and oxymyoglobin. The porphyrin core of oxyperoxidase is slightly more expanded with the iron atom closer to the porphyrin plane, and there is greater iron d pi-to-oxygen pi backbonding compared to oxymyoglobin. The iron-oxygen (stretching or bending) bands are observed at 570 and 562 cm-1, respectively, for oxymyoglobin and oxyperoxidase, and the iron-His stretching bands have been tentatively identified at 276 and 289 cm-1, respectively. It is suggested that the stronger iron-His bond in oxyperoxidase facilitates greater iron d pi-to-oxygen pi backdonation by raising the energy of the iron d pi orbitals closer to the energy of the oxygen pi orbitals. This weakens the O-O bond and activates dioxygen for use as an electron acceptor in the peroxidase-oxidase reaction.

Horseradish Peroxidase↗
PubMed1999

New chemiluminescence assay for linamarin.

A new chemiluminescence assay was developed for the quantitative determination of linamarin, a cyanogenic glucoside present in cassava. The assay involved hydrolysis of linamarin by a specific enzyme, linamarase, to release glucose, which was then quantitated by a chemiluminescence system consisting of glucose oxidase-peroxidase-luminol. The new assay was more sensitive than the conventional spectrophotometric method for quantitating linamarin in cassava extracts. However, the following agents were found to interfere with the new assay: Vanadate, Mg2+, and Cu2+, were inhibitory to the luminescence of the H2O2-peroxidase-luminol system used in the coupling reaction, whereas EDTA and EGTA activated the system. In addition, Hg2+, which inhibits glucose oxidase, and Tris ion, which inhibits linamarase, both interfered with the new assay.

Evaluation Studies as Topic↗
PubMed1977

A new colorimetric method for determination of serum glucose.

A new colorimetric method using 4-aminoantipyrine-dimethylaniline in a glucose oxidase-peroxidase system is proposed to determine glucose in serum. The developed color was stable at the optimum pH of glucose oxidase, 5.6. The method is more sensitive than the o-dianisidine method and is reproducible. The correlation between the proposed method and the o-dianisidine method is 0.989.

Aniline Compounds↗
PubMed1986

Cytochemical expression of epidermal peroxidase and cytochrome oxidase activities in pathological skin conditions of man.

The cytochemical expression of epidermal peroxidase and cytochrome oxidase activity was recently well documented in normal human skin. We report here its expression in basal and squamous cell carcinomas, actinic keratoses, psoriasis, allergic contact dermatitis, seborrheic keratoses, and autosomal dominant ichthyosis vulgaris. The two enzyme activities were evaluated using the diaminobenzidine method. If present, the two enzymes were always localized in the same organelles as in normal epidermis: endogenous peroxidase in the nuclear envelope and endoplasmic reticulum, and cytochrome oxidase in mitochondria. In basal and squamous carcinomas, actinic keratoses and psoriasis, the keratinocytes lost their peroxidase activity, but maintained their cytochrome oxidase activity. In seborrheic keratoses, allergic contact dermatitis and ichthyosis vulgaris, the cytochrome oxidase activity was greatly reduced or abolished in keratinocytes, Langerhans' cells, and melanocytes, whereas the peroxidase activity was present as in normal epidermis. These results indicate that the two peroxidatic enzymes studied are not interrelated and alternatively suppressed by different cellular dysfunctions.

3,3'-Diaminobenzidine↗
PubMed1989

The streptococcal flavoprotein NADH oxidase. I. Evidence linking NADH oxidase and NADH peroxidase cysteinyl redox centers.

The FAD-containing NADH oxidase from Streptococcus faecalis 10C1, which catalyzes the four-electron reduction of O2----2H2O, has been purified by an improved procedure for analyses of its structural and redox properties. The enzyme is apparently a dimer of two identical subunits, each containing 1 mol of FAD. Dithionite reduction of the enzyme proceeds in two distinct phases corresponding to approximately 0.5 and 1.1 eq/FAD, respectively. Thiol assays of the NADH oxidase, reduced anaerobically with 1 eq of NADH/FAD prior to denaturation, are consistent with the presence of a single redox-active cysteinyl residue/subunit. Analysis of the cysteinyl peptides of the oxidase, identified in tryptic digests of the enzyme labeled metabolically with [35S]cysteine, reveals a sequence which is closely related to the redox-active cysteinyl peptide sequence recently determined for the streptococcal flavoprotein NADH peroxidase. A second cysteinyl peptide sequence, when aligned with residues 3-17 of the peroxidase NH2-terminal sequence, reveals identity in 7 of 15 positions and satisfies several of the criteria described for ADP-binding structures. Additional probes of the structural and redox properties of the NADH oxidase, including visible circular dichroism spectroscopy and sensitivity to inactivation by hydrogen peroxide, provide further evidence for a fundamental structural connection between flavin-dependent NADH oxidase and peroxidase functions.

Amino Acid Sequence↗
PubMed1981

Enzymatic determination of lipoprotein-X, a specific serum cholestasis marker.

Non-esterified cholesterol was determined enzymatically with the cholesterol oxidase-peroxidase reaction using phenol and 4-aminophenazone as chromogens. This assay as done in the supernatant containing the lipoprotein-X. Other serum lipoproteins were removed by precipitation with heparin and zinc acetate followed by centrifugation. No standardization was required, the lipoprotein-X concentration being calculated with the use of the constant.

Cholestasis↗
PubMed1988

Thiols as myeloperoxidase-oxidase substrates.

Nine low-Mr thiols were compared with regard to their ability to function as myeloperoxidase-oxidase substrates under conditions where no auto-oxidation of the thiols could be observed. The methyl and ethyl esters of cysteine were found to be about twice as active as cysteamine at pH 7.0, in terms of increased O2 consumption. Cysteine itself was poorly active, whereas glutathione, N-acetylcysteine and penicillamine were completely inactive as myeloperoxidase-oxidase substrates under these conditions. The structure-activity relationships indicated that both a free thiol and free amino group were required for peroxidase-oxidase activity, and also that a free carboxy group abolished activity. In analogy with cysteamine, the activities of both cysteine esters were inhibited by superoxide dismutase (less than 5 micrograms/ml) and by catalase and not by the hydroxyl-radical scavenger mannitol. In contrast with cysteamine, the activities of both cysteine esters were stimulated more than 2-fold by high concentrations (greater than 5 micrograms/ml) of superoxide dismutase. The activities of both cysteine esters exhibited broad pH optima at pH 7. A mechanism for the myeloperoxidase-oxidase oxidation of the cysteine esters is proposed, which is partly different from that previously proposed for cysteamine.

Catalase↗
PubMed2003

A model of the oscillatory metabolism of activated neutrophils.

We present a two-compartment model to explain the oscillatory behavior observed experimentally in activated neutrophils. Our model is based mainly on the peroxidase-oxidase reaction catalyzed by myeloperoxidase with melatonin as a cofactor and NADPH oxidase, a major protein in the phagosome membrane of the leukocyte. The model predicts that after activation of a neutrophil, an increase in the activity of the hexose monophosphate shunt and the delivery of myeloperoxidase into the phagosome results in oscillations in oxygen and NAD(P)H concentration. The period of oscillation changes from >200 s to 10-30 s. The model is consistent with previously reported oscillations in cell metabolism and oxidant production. Key features and predictions of the model were confirmed experimentally. The requirement of the hexose monophosphate pathway for 10 s oscillations was verified using 6-aminonicotinamide and dexamethasone, which are inhibitors of glucose-6-phosphate dehydrogenase. The role of the NADPH oxidase in promoting oscillations was confirmed by dose-response studies of the effect of diphenylene iodonium, an inhibitor of the NADPH oxidase. Moreover, the model predicted an increase in the amplitude of NADPH oscillations in the presence of melatonin, which was confirmed experimentally. Successful computer modeling of complex chemical dynamics within cells and their chemical perturbation will enhance our ability to identify new antiinflammatory compounds.

Catalysis↗
PubMed1993

A reagentless amperometric biosensor for alcohol detection in column liquid chromatography based on co-immobilized peroxidase and alcohol oxidase in carbon paste.

A reagentless carbon paste electrode chemically modified with covalently bound alcohol oxidase and horse-radish peroxidase was examined as a selective sensor in flow injection and column liquid chromatography. A combination of carbodiimide, glutaraldehyde, and polyethyleneimine was used for immobilizing the enzymes in the paste. The surface of the electrodes was protected by first forming a layer of electropolymerized ortho-phenylenediamine followed by deposition of a cation exchange membrane (Eastman AQ 29D). The electrodes were used for detection of hydrogen peroxide, methanol, ethanol, propanol, isopropanol, and butanol. Preliminary investigations of the use of this sensor for bioprocess control are reported.

Alcohol Oxidoreductases↗
PubMed1990

Glyoxal oxidase of Phanerochaete chrysosporium: its characterization and activation by lignin peroxidase.

Glyoxal oxidase (GLOX) is an extracellular H2O2-generating enzyme produced by ligninolytic cultures of Phanerochaete chrysosporium. The production, purification, and partial characterization of GLOX from agitated cultures are described here. High-oxygen levels are critical for GLOX production as for lignin peroxidase. GLOX purified by anion-exchange chromatography appears homogeneous by NaDod-SO4/PAGE (molecular mass = 68 kDa). However, analysis by isoelectric focusing indicates two major bands (pI 4.7 and 4.9) that stain as glycoproteins as well as for H2O2-producing activity in the presence of methylglyoxal. Purified GLOX shows a marked stimulation in activity when incubated with Cu2+; full activation takes more than 1 hr with 1 mM CuSO4 at pH 6. The steady-state kinetic parameters for the GLOX oxidation of methylglyoxal, glyceraldehyde, dihydroxyacetone, glycolaldehyde, acetaldehyde, glyoxal, glyoxylic acid, and formaldehyde, were determined by using a lignin peroxidase coupled-assay at pH 4.5. Of these substrates, the best is the extracellular metabolite methylglyoxal with a Km of 0.64 mM an apparent rate of catalysis, kcat, of 198 s1 under air-saturated conditions. The Km for oxygen is greater than the concentration of oxygen possible at ambient pressure--i.e., >1.3 mM at 25 degrees C. Importantly, oxygen-uptake experiments show that purified GLOX is inactive unless coupled to the peroxidase reaction. With this coupled reaction, for each mol of methylglyoxal, veratryl alcohol (a lignin peroxidase substrate), and oxygen consumed, 1 mol each of pyruvate and veratraldehyde is produced. The importance of these results is discussed in relation to the physiology of lignin biodegradation and possible extracellular regulatory mechanisms for the control of oxidase and peroxidase activities.

Journal Article↗
PubMed1983

Geometry and orientation of neuronal processes in cat primary auditory cortex (AI) related to characteristic-frequency maps.

Microelectrode mapping and horseradish peroxidase oxidase histochemistry were combined to study the relationship between the characteristic-frequency representation and the intrinsic connectivity of the primary auditory cortex in the cat. Small extracellular iontophoretic injections of horseradish peroxidase within the characteristic-frequency map resulted in labeling of neuronal processes that, in the tangential plane, radiated out asymmetrically from the injection site over distances of several millimeters. The heaviest concentration of labeled fibers was along an axis parallel with the orientation of the isofrequency line within which the injection had been made. Thus, primary field neurons that have the same or a similar characteristic frequency have the potential of being preferentially interconnected.

Animals↗
PubMed1975

[Automatic assay of blood sugar by Trinder's method].

An automated method for determining blood "true glucose" has been adapted to the single channel "AutoAnalyzer". The action of the glucose-oxidase peroxidase system is directly coupled with an oxygen acceptor chromogen. The validity for accuracy, contamination and the absence of interferences by certain compounds have been tested. Experimenters proceeded then with a thorough examination of the relation existing between the "true glucose" determined by the present method combined with the Hexokinase method and the "true guclose" determined with the Beckman "Glucose Analyzer".

Autoanalysis↗
PubMed1964

AN EVALUATION OF SOME COMMERCIAL TEST PAPERS AND TABLETS FOR THE DETERMINATION OF GLUCOSE IN URINE.

The commercial test papers, Tes-Tape, Clinistix, Uristix and Combistix, and the tablet preparation, Clinitest, were evaluated as indicators of glucose in urine by means of a quantitative automated glucose oxidase procedure for glucose determination. The semiquantitative Tes-Tape yielded very low values on urine specimens when compared with the quantitative method. More reliable results could be obtained with this product if the urine specimens were first treated with a mixed bed resin to remove inhibitors of the glucose oxidase peroxidase system. The qualitative test papers, Clinistix, Uristix and Combistix, yielded responses in closer agreement with the automated data, the best performance being obtained with Clinistix. The semiquantitative Clinitest tablets generally yielded more accurate results on a direct urine test than did Tes-Tape, although the Clinitest tablet is designed to measure total reducing substances rather than glucose alone.

Citric Acid↗