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At least 667 records · Page 37Linked to original sources
PubMed1982

[Determination of total serum phospholipids by a new enzymatic colorimetric method: statistical quality control].

Enzymatic methods have progressively substituted extractive procedures in plasma lipids determination. A new enzymatic method for serum phospholipids evaluation has been recently introduced in Italy as a kit of reagents. In this method phospolipase D hydrolyzes phospholipids with free choline production which, in presence of choline-oxidase and peroxidase, is estimated by colorimetric reaction. Linearity of response and analytical variations "within-run" and "between-run" during six month observations on serum pools have been preliminarily verified.

Choline↗
PubMed1980

Continuous-flow fluorometry of low galactose concentrations in blood or plasma.

Clearance of 0-100 mg/L concentrations of galactose from the blood depends on nutrient hepatic blood flow. We can measure such concentrations, which was not previously possible, by a continuous-flow method involving the use of galactose oxidase and peroxidase, the latter being coupled to a fluorogenic substrate, p-hydroxyphenylacetic acid. Interfering substances in the peroxidase reaction are removed by zinc/alkali precipitation. Sensitivity is maximized by using saturating concentrations of the enzymes and substrate. In prepared plasma test samples with galactose concentrations of 10, 40, 70, and 100 mg/L, the within-run CV's ranged from 2.1 to 8.6%, and day-to-day CV's from 2.2 to 17.2%, the largest CV's being for the 10 mg/L concentration. Normal subjects are shown to clear galactose more efficiently than subjects with moderate cirrhosis.

Anticoagulants↗
PubMedDate not supplied

[Induction of plant resistance to the tobacco mosaic virus with a double-stranded poly(G)-poly(C) complex].

Inoculation of double-stranded polyribonucleotide poly(G) . poly(C) complex in a concentration of 50-200 micrograms/mg into tobacco and thornapple leaves was found to produce resistance of the plants to subsequent infection with tobacco mosaic virus (TMV) manifested in decreased number and size of local virus lesions. The induced resistance may spread over the plant and be found in the upper untreated leaves. The level of systemic resistance, however, is much lower than that of the resistance demonstrated in the injected leaves. Actinomycin D (5 micrograms/ml) had no significant effect on the number but stimulated the growth of lesions developing in leaves injected with poly(G) . poly(C) as well as increased their number in the upper leaves of the same plants proximal to the treated ones. Development of tobacco resistance to TMV was accompanied by changes in the activity of terminal oxidases, particularly peroxidase. Possible mechanisms of formation of induced resistance are discussed.

Plant Diseases↗
PubMedDate not supplied

N-hydroxylation of the antiprotozoal drug pentamidine catalyzed by rabbit liver cytochrome P-450 2C3 or human liver microsomes, microsomal retroreduction, and further oxidative transformation of the formed amidoximes. Possible relationship to the biological oxidation of arginine to NG-hydroxyarginine, citrulline, and nitric oxide.

Previous investigations have shown that the antiprotozoal drug pentamidine is N-hydroxylated by rabbit and rat liver microsomal fractions. Indirect evidence for the participation of the cytochrome P-450 enzyme system was obtained. In this study, rabbit liver cytochrome P-450 2C3 is shown by reconstitution experiments with highly purified variants of P-450 2C3 isolated from rabbit liver and purified variants of P-450 2C3 expressed by recombinant Escherichia coli to be a microsomal pentamidine N-hydroxylase. The two variants, P-450 2C3 (6 beta H) and P-450 2C3 (6 beta L), are equally efficient for the formation of the monoamidoxime derivative of pentamidine. N-hydroxypentamidine is further oxidized to the respective amide by reconstituted rabbit liver P-450 enzyme systems involving the oxidase and peroxidase activities of this enzyme. Formation of nitric oxide [(NO); endothelium-derived relaxing factor] during this oxidation is shown by the detection of the cytochrome P-420-Fe(II)-NO complex by visible difference spectroscopy. The possibility for the N-hydroxylation of pentamidine to the corresponding amidoximes and subsequent oxidative conversion to the respective amide derivatives is comparable with the physiological transformation of arginine to citrulline via N-hydroxyarginine with liberation of NO (endothelium-derived relaxing factor). The N-hydroxylated derivatives of pentamidine are easily retroreduced by microsomal fractions from rabbit liver. NADH is preferred to NADPH as cofactor for this reduction, and the reaction is strongly suppressed by the addition of N-methylylhydroxylamine. The N-hydroxylation of pentamidine and the retroreduction are also catalyzed by human liver microsomes.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1993

Changes in phospholipids, fatty acids, oxidative enzymes, phenolics and protein levels during growth of normal and habituated tissues of Cocculus pendulus.

Cultures of C. pendulus were maintained on hormone free and hormone supplemented (NAA 1.0 mg/l and kinetin 0.5 mg/l) Murashige and Skoog medium. During the growth period, hormone free cultures had higher phenolic content, polyphenol oxidase activity and less protein content, peroxidase and IAA oxidase activity. Activity of all the three oxidising enzymes and phenolic content were high at 16 days growth. Total lipid content was higher (2.7-folds at 15 days) in hormone free cultures. Phospholipid content of both cultures was not markedly dissimilar except PC and DGDG contents. Thus it is evidenced that both the tissues were similar metabolically.

Alkaloids↗
PubMed1993

[Enzymatic determination of cholesterol in bile without interference of bilirubin].

The authors describe an enzymatic method for cholesterol determination in bile after elimination of bilirubin interference. During sample pretreatment, bilirubin is oxidized by hydrogen peroxide produced by adding glucose, glucose oxidase and peroxidase. Excess hydrogen peroxide is oxidatively coupled with 4-amino-antipyrine and a phenolic derivative (P-hydroxybenzoic acid). Cholesterol is then measured by use of a CHOD-PAP kinetic fixed-time method adapted to two different centrifugal analyzers (Multistat and Monarch IL). This method has a good within-run precision (CV = 1.6%) and good linearity (up to 23 mmol/l). Results have been compared to gas-liquid chromatographic (method selected by the Lipids-Lipoproteins Commission of the SFBC). The allometric regression line is: y = 1.016 x - 0.07 with r = 0.9975 (P < 0.001).

Bile↗
PubMed1993

Clinical and analytical evaluation of a continuous enzymatic method for measuring pancreatic lipase activity.

We report the evaluation of a new commercial kit for the determination of pancreatic lipase activity. The kit is based on the use of a 1,2-diglyceride as substrate and a specific monoglyceride lipase. The detection step is the continuous colorimetric measurement of hydrogen peroxide produced from glycerol by glycerol kinase, glycerol-3-phosphate oxidase, and peroxidase reactions. The procedure appears to be precise (between-day CV < 9%) and the results show good correlation with those obtained by alternative procedures (vs turbidimetry, r = 0.965; vs ultraviolet absorbance-enzymatic method, r = 0.995; vs Ektachem, r = 0.976; vs immunometry, r = 0.970). However, the method is susceptible to interference by increased concentrations (> 4.5 mmol/L) of serum triglycerides. We estimated the reference interval for healthy adults to be 8-44 U/L. When we evaluated clinical efficacy by using receiver-operating characteristic curves and the overlap index, no significant differences were found between the commercial kit and a common turbidimetric assay for diagnosing patients with acute pancreatitis; both methods performed satisfactorily.

Adult↗
PubMedDate not supplied

[Potentiometric electrodes for determining choline, butyrylcholine and cholinesterase inhibitors].

Potentiometric choline electrodes were developed on the basis of the mediator-free bioelectrocatalysis. The electrodes made of a composite carbon-polymer material contain choline oxidase and peroxidase coimmobilized on the surface of the electrode. The rate of the potential increase was shown to be proportional to the choline concentration within a broad range of variation. Coupling of choline-sensitive electrodes with butyrylcholinesterase makes possible both the direct detection of butyrylcholine and analysis of butyrylcholinesterase inhibitors.

Butyrylcholinesterase↗
PubMed1987

The Effect of Pseudomonas putida Colonization on Root Surface Peroxidase.

Increased activities of peroxidase and indole 3-acetic acid (IAA) oxidase were detected on root surfaces of bean (Phaseolus vulgaris) seedlings colonized with a soil saprophytic bacterium, Pseudomonas putida. IAA oxidase activity increased over 250-fold and peroxidase 8-fold. Enhancement was greater for 6-day-old than for 4- or 8-day-old inoculated plants No IAA oxidase or peroxidase activities were associated with the bacterial cells. Native polyacrylamide gel electrophoresis demonstrated that washes of P. putida-inoculated roots contained two zones of peroxidase activity. Only the more anodic bands were detected in washes from noninoculated roots. Ion exchange and molecular sizing gel chromatography of washes from P. putida-colonized roots separated two fractions of peroxidase activity. One fraction corresponded to the anodic bands detected in washes of P. putida inoculated and in noninoculated roots. A second fraction corresponded to the less anodic zone of peroxidase, which was characteristic of P. putida-inoculated plants. This peroxidase had a higher IAA oxidase to peroxidase ratio than the more anodic, common enzyme. The changes in root surface peroxidases caused by colonization by a saprophytic bacterium are discussed with reference to plant-pathogen interactions.

Journal Article↗
PubMed2001

Phenols and phenol oxidases are involved in cadmium accumulation in the water plants Nymphoides peltata (Menyanthaceae) and Nymphaeae (Nymphaeaceae).

This comparative study investigates the mechanism of cadmium accumulation in the semiaquatic plant Nymphoides peltata (Menyanthaceae) and the aquatic plant Nymphaea (Nymphaeaceae). It was conducted as part of an ongoing study of the use of water plants for phytoremediation. Epidermal structures, known as hydropotes, are located on the abaxial epidermis of the leaf laminae of Nymphoides peltata and are shown to contain phenols, peroxidase and polyphenol oxidase activities. When plants are subjected to 50 mg/l of cadmium in the growth medium, these hydropotes accumulate cadmium. Cadmium-induced increases in phenols, peroxidase and polyphenol oxidase activities were determined in plant extracts. Cadmium binding by polymerized phenols was demonstrated in vivo. In comparison with Nymphaeae epidermal glands, N. peltata hydropotes are larger, open, and create bigger crystal, the latter principally composed of calcium and, proportionally, less cadmium. Although both plants showed similar levels of cadmium accumulation, N. peltata was sensitive while Nymphaeae was resistant to this cadmium level. It is suggested that in these water plants the main mechanism for cadmium accumulation is based on the trapping of cadmium crystals by polymerized phenols in specialized epidermal structures and this is due to peroxidase and polyphenol oxidase activities. Nymphaeae, with greater peroxidase activity and more polyphenols, is more resistant to this heavy metal than N. peltata.

Biodegradation, Environmental↗
PubMed2006

Roles for Arg426 and Trp111 in the modulation of NADH oxidase activity of the catalase-peroxidase KatG from Burkholderia pseudomallei inferred from pH-induced structural changes.

Crystals of Burkholderia pseudomallei KatG retain their ability to diffract X-rays at high resolution after adjustment of the pH from 5.6 to 4.5, 6.5, 7.5, and 8.5, providing a unique view of the effect of pH on protein structure. One significant pH-sensitive change lies in the appearance of a perhydroxy group attached to the indole nitrogen of the active site Trp111 above pH 7, similar to a modification originally observed in the Ser324Thr variant of the enzyme at pH 5.6. The modification forms rapidly from molecular oxygen in the buffer with 100% occupancy after one minute of soaking of the crystal at room temperature and pH 8.5. The low temperature (4 K) ferric EPR spectra of the resting enzyme, being very sensitive to changes in the heme iron microenvironment, confirm the presence of the modification above pH 7 in native enzyme and variants lacking Arg426 or Met264 and its absence in variants lacking Trp111 or Tyr238. The indole-perhydroxy group is very likely the reactive intermediate of molecular oxygen in the NADH oxidase reaction, and Arg426 is required for its reduction. The second significant pH-sensitive change involves the buried side chain of Arg426 that changes from one predominant conformation at low pH to a second at high pH. The pH profiles of the peroxidase, catalase, and NADH oxidase reactions can be correlated with the distribution of Arg426 conformations. Other pH-induced structural changes include a number of surface-situated side chains, but there is only one change involving a displacement of main chain atoms triggered by the protonation of His53 in a deep pocket in the vicinity of the molecular 2-fold axis.

Arginine↗
PubMed1985

Rat intestinal peroxidase: inhibition by endogenous xanthine and xanthine oxidase.

The high-speed supernatant from homogenates of rat small intestine contains a heat-stable, dialyzable factor which showed a time-dependent inhibition of peroxidase activity in salt extracts of the tissue. The inhibitor was purified by chromatography on Dowex 50W-X8 and identified as xanthine. The inhibition of peroxidase by xanthine was prevented by allopurinol, an inhibitor of xanthine oxidase, and hypoxanthine was also found to be inhibitory. H2O2, produced in the reaction catalyzed by xanthine oxidase, was shown to be directly responsible for the observed inhibition. The time-dependent loss of peroxidase activity in the presence of xanthine or hypoxanthine occurred more rapidly in NH4Cl than in CaCl2 extracts of small intestine and was due to the difference in the initial concentration of H2O2 in these two extracts. The possible relationship between peroxidase and xanthine oxidase in the rat small intestine is discussed.

Allopurinol↗
PubMed1991

Overproduction of lignin-degrading enzymes by an isolate of Phanerochaete chrysosporium.

Phanerochaete chrysosporium is a white rot fungus which secretes a family of lignin-degrading enzymes under nutrient limitation. PSBL-1 is a mutant of this organism that generates the ligninolytic system under nonlimiting conditions during primary metabolism. Lignin peroxidase, manganese peroxidase, and glyoxal oxidase activities for PSBL-1 under nonlimiting conditions were 4- to 10-fold higher than those of the wild type (WT) under nitrogen-limiting conditions. PSBL-1 was still in the log phase of growth while secreting the enzymes, whereas the WT had ceased to grow by this time. As in the WT, manganese(II) increased manganese peroxidase activity in the mutant. However, manganese also caused an increase in lignin peroxidase and glyoxal oxidase activities in PSBL-1. Addition of veratryl alcohol to the culture medium stimulated lignin peroxidase activity, inhibited glyoxal oxidase activity, and had little effect on manganese peroxidase activity in PSBL-1, as in the WT. Fast protein liquid chromatography (FPLC) analysis shows production of larger amounts of isozyme H2 in PSBL-1 than in the WT. These properties make PSBL-1 very useful for isolation of large amounts of all ligninolytic enzymes for biochemical study, and they open the possibility of scale-up production for pratical use.

Alcohol Oxidoreductases↗
PubMed2002

Mesopone cytochrome c peroxidase: functional model of heme oxygenated oxidases.

The effect of heme ring oxygenation on enzyme structure and function has been examined in a reconstituted cytochrome c peroxidase. Oxochlorin derivatives were formed by OsO(4) treatment of mesoporphyrin followed by acid-catalyzed pinacol rearrangement. The northern oxochlorin isomers were isolated by chromatography, and the regio-isomers assignments determined by 2D COSY and NOE 1H NMR. The major isomer, 4-mesoporphyrinone (Mp), was metallated with FeCl(2) and reconstituted into cytochrome c peroxidase (CcP) forming a hybrid green protein, MpCcP. The heme-altered enzyme has 99% wild-type peroxidase activity with cytochrome c. EPR spectroscopy of MpCcP intermediate compound I verifies the formation of the Trp(191) radical similar to wild-type CcP in the reaction cycle. Peroxidase activity with small molecules is varied: guaiacol turnover increases approximately five-fold while that with ferrocyanide is approximately 85% of native. The electron-withdrawing oxo-substitutents on the cofactor cause a approximately 60-mV increase in Fe(III)/Fe(II) reduction potential. The present investigation represents the first structural characterization of an oxochlorin protein with X-ray intensity data collected to 1.70 A. Although a mixture of R- and S-mesopone isomers of the FeMP cofactor was used during heme incorporation into the apo-protein, only the S-isomer is found in the crystallized protein.

Cloning, Molecular↗
PubMed2004

Reactive oxygen and ethylene are involved in the regulation of regurgitant-induced responses in bean plants.

Application of regurgitant from Leptinotarsa decemlineata Say on wound surfaces of one wounded leaf of intact bean (Phaseolus vulgaris L.) plants resulted in activation of ethylene biosynthesis followed by an increase of both peroxidase and polyphenol oxidase activity. The aim of the present investigation was to study the source of increased oxidative enzyme activities in regurgitant-treated bean leaves and to determine if hydrogen peroxide and ethylene biosynthesis is responsible for regurgitant-induced amplification of wound responses in bean plants. As the regurgitant contained relative high activities of both peroxidase and polyphenol oxidase, there is a possibility that increased enzyme activities in bean leaves following regurgitant treatment is an artifact of insect-derived enzymes. Localisation experiments and electrophoretic analysis revealed that only part of the increased enzyme activities could be attributed to regurgitant-derived enzymes. Both increase of ethylene production and oxidative enzyme activities depended on protein synthesis. To demonstrate if the increase of oxidative metabolism was ethylene-dependent, seedlings were pretreated with aminooxyacetic acid, an inhibitor of ethylene biosynthesis, and 1-methylcyclopropene (1-MCP), a competitive inhibitor of ethylene action. Increase of both peroxidase and polyphenol oxidase activity in wounded and subsequently regurgitant-treated leaf was abolished by both aminooxyacetic acid and 1-MCP. Inhibitor studies indicated that H2O2 generated through NADPH oxidase and superoxide dismutase is necessary for regurgitant-induced increase of ethylene production and oxidative enzyme activities.

Aminooxyacetic Acid↗