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PubMed1977

[Synthesis and properties of carrier-fixed enzymes. VIII. Kinetic studies of the binding velocity of enzymes to macroporous carriers].

The kinetics of binding the enzymes glucose oxidase, trypsin, and peroxidase and also bovine gamma-globulin to the macroporous carriers dialdehyde cellulose, diazotized amino polystyrene, acrolein-acrylamide copolymer, and isothiocyanate groups carrying CPG-glass was studied. It was found empirically that the increase in protein content and--if there occurred no inactivation of enzyme during binding reaction--of enzymatic activity of the enzyme-carrier complex with the reaction time can be described by saturation curves (first order hyperbolas), which represent straight lines after suitable transformation. Thereby it is possible to calculate protein content or specific activity of the enzyme-carrier complex for any moment during binding reaction. From intercepts of the obtained straight lines with the ordinate and with the abscissa, respectively, one can determine the maximum binding capacity and the maximum specific activity and from their slope the reaction rate can be obtained. If there result no straight lines for plotting enzymatic activity of the enzyme-carrier complex against binding time after transformation, then this is an indication for partial inactivation of the free or already insolubilized enzyme. From kinetic measurements it is concluded that in all cases studied by use the preceding stage in chemical fixation of the enzyme to carrier is an adsorption equilibrium. Limitation of reaction rate by diffusion as in loading an ion exchanger could not be observed.

Glass↗
PubMed1976

[Experimental revascularization of acute myocardial infarction. II: Activity of various oxidoreductive tissutal and serum enzymes (author's transl)].

The behaviour of some enzymatic activities, such as monoamino oxidase (MAO), diamino oxidase (DAO), catalase, peroxidase and creatin chinase (CPK) have been studied both in blood serum and myocardial tissue of acute infarcted dogs (obtained by coronary occlusion). The most significant results are the changes of the DAO activity (--50% from the control) and peroxidase activity (+60%), 6 hours after acute ischemia. The effect of reperfusion was studied 2 hours later. A recovery of DAO activities was shown, while the peroxidase activities stayed elevated. All the enzymatic activities studied were evaluated in the serum, under the same experimental conditions. An increase of all these activities was observed until 6th hour of coronary occlusion. The reperfusion of acute ischemia, after six hours, causes a further increase of CPK and MAO activities and a decrease of catalase peroxidase and particulary evident DAO activities. The results of this experiment show that reoxygenation, under our experimental conditions, increases a further enzymatic release and in part causes a metabolic recovery of heart muscle.

Amino Acid Oxidoreductases↗
PubMed1989

Simple enzymatic determination of total cholesterol in gallstones.

In this simple method for rapid enzymatic determination of total cholesterol in human gallstones, gallstone powder is dissolved in an 80/20 by vol mixture of N,N-dimethylformamide and dimethyl sulfoxide and reacted directly with the aqueous enzymatic reagent, without further treatment. The organic solvents do not interfere with enzymatic activities of cholesterol oxidase, esterase, and peroxidase in the assay mixture. The method is reproducible (CVs 3.7% to 6.6%), analytical recoveries ranged from 98.6% to 102%, and linearity is good. Furthermore, results correlated well with those obtained by infrared spectroscopic measurements.

Cholelithiasis↗
PubMed1989

Developmental biology of oxidant-producing enzymes and antioxidants in the piglet intestine.

The pathogenesis of neonatal necrotizing enterocolitis is unknown, but a possible role for reactive oxygen metabolites has been postulated. We evaluated whether developmental differences exist in the levels of 1) the free radical-generating enzyme xanthine oxidase, 2) granulocyte peroxidase, an index of the resident granulocyte population, 3) free radical-scavenging enzymes (superoxide dismutase, catalase, and glutathione peroxidase), and 4) reduced glutathione, an endogenous antioxidant, in the ileal and colonic mucosa of 1-d-old, 3-d-old, 2-wk-old, and 1-mo-old piglets. We found no xanthine dehydrogenase/oxidase activity in 1-d to 1-mo-old piglets. Mucosal granulocyte peroxidase activity was higher in older animals, indicating that there was an age-dependent infiltration of granulocytes (eosinophils, neutrophils) in the distal bowel. The peroxidase activity per circulating granulocyte, however, did not vary with age. Superoxide dismutase activity was significantly higher in 1-d-old piglets than in all older age groups; glutathione peroxidase activity was significantly lower in 1-d-old animals than that of older age groups. There was no detectable catalase activity in the mucosa when tissue was corrected for catalase activity of blood. Finally, ileal GSH levels were significantly lower in 1-d-old than in 2-wk-old and 1-mo-old animals, whereas colonic reduced glutathione activity did not differ among age groups. In conclusion, the distal bowel of the neonatal piglet appears to have a limited capacity to generate oxidants via xanthine oxidase and resident granulocytes. However, the neonatal piglet intestine has a lower capacity to detoxify hydrogen peroxide than that of older animals.

Animals↗
PubMed1996

Tissue printing for peroxidases associated with lignification.

Peroxidases with syringaldazine oxidase activity have been claimed to be specifically involved in lignification. The use of syringaldazine as a substrate presents problems of color diffusion and fading. We report a method for timing color development of syringaldazine peroxidase reactions in tissue prints, and conditions under which diffusion is minimized. The best time interval in which the tissue print and background gave significant contrast was determined using ELISA plates in which impressions of the tissue could be made, mimicking reactions on a membrane. This technique permitted simultaneous reading of a large number of samples and blanks, rendering enough data points for statistical analysis. Optimum development time for syringaldazine peroxidase reactions was between 10 and 20 min. Color diffusion and smearing of syringaldazine peroxidase reactions in tissue prints were minimized when prints were covered with a strip of membrane before adding the substrate mixture.

Brassica↗
PubMed2005

Biochemical study of leaf browning in minimally processed leaves of lettuce (Lactuca sativa L. var. acephala).

A series of biochemical parameters, including the concentration of total ascorbic acid (ASA(tot)) and the activities of phenylalanine ammonia lyase (PAL), polyphenol oxidase (PPO), and peroxidases (PODs), was investigated during cold storage (72 h at 4 degrees C in the dark) in fresh-cut (minimally processed) leaves of two lettuce (Lactuca sativa L. var. acephala) cultivars differing in the susceptibility to tissue browning: Green Salade Bowl (GSB), susceptible, and Red Salade Bowl (RSB), resistant. The two cultivars showed differences also at the biochemical level. The content in ASA(tot) increased in RSB, as a consequence of increased DHA concentration; conversely, ASA(tot) diminished in GSB, in which ASA was not detectable after 72 h of storage, thus suggesting a disappearance of ascorbate (both ASA and DHA) into nonactive forms. The antioxidant capacity (as determined by using FRAP analysis) decreased significantly during storage in RSB, while a strong increase was observed in GSB. PAL activity increased soon after processing reaching a maximum by 3 h, then it declined to a relatively constant value in RSB, while in GSB it showed a tendency to decrease in the first few hours from harvest and processing. POD activity, at least for chlorogenic acid, increased significantly during storage only in GSB.

Antioxidants↗
PubMed2004

Effect of different washing procedures on phenolic metabolism of shredded, packaged iceberg lettuce during storage.

Different washing treatments applying chlorinated, ozonated, and tap water were examined for their effect on the phenolic metabolism of minimally processed iceberg lettuce (Lactuca sativa L.) during storage in consumer-sized bags at 4 degrees C for up to 9 days. To eliminate problems associated with raw material inhomogeneity, processing was conducted on a pilot-plant scale under operating conditions of industrial practice. Inherent product heterogeneity caused by diverse lettuce leaf tissues was compensated for by pooling large-sized samples, and frequent sampling ensured significant data about the activities of phenylalanine ammonia-lyase (PAL), polyphenol oxidase (PPO), and peroxidase (POD), as well as the contents of caffeic acid derivatives over storage time. In the homogeneous lettuce samples, specific responses caused by different washing procedures were detectable. PAL activity in the samples increased for up to 5-8 days of storage. Compared to tap and ozonated water, the use of chlorinated water (100-200 mg/L free chlorine) for washing trimmed heads or shredded lettuce significantly reduced PAL activity and the concomitant rise of 3,5-di-O-caffeoylquinic acid (isochlorogenic acid isomer) concentrations. The phenolic acids O-caffeoyltartaric (caftaric acid), di-O-caffeoyltartaric (chicoric acid), 5-O-caffeoylquinic (chlorogenic acid isomer), and O-caffeoylmalic were less influenced by different washing treatments. Individual contents either were constant or decreased during storage. Additionally, the novel finding of a further caffeic acid isomer, tentatively identified as meso-di-O-caffeoyltartaric acid, is reported. PPO and POD activities were less affected by different washing treatments and thus were less suitable physiological indicators of stress reactions triggered by alternative processing.

Caffeic Acids↗
PubMed1988

Cytochrome oxidase staining marks dendritic zones of the rat olfactory bulb external plexiform layer.

Cytochrome oxidase staining of the rat olfactory bulb external plexiform layer (EPL) produces a darkly stained intermediate zone bordered by lightly stained superficial and deep zones. Similar zonal staining was seen in cats, rabbits, and hamsters. These zones vary in relative thickness around the circumference of the olfactory bulb; the deep zone is proportionally thicker in the most dorsal and ventral parts of the bulb. Tufted cell somata are unevenly distributed within the EPL; the outer part of the EPL has more somata. The distribution of the cytochrome oxidase reaction product shows that the darkly stained intermediate zone is not produced by staining of tufted cell somata. Zones of cytochrome oxidase staining correspond to the sublaminar distribution of mitral and tufted cell basal dendrites. This was demonstrated by labeling mitral and tufted cells with small extracellular horseradish peroxidase injections and processing alternate sections for horseradish peroxidase and for cytochrome oxidase. Because there was cross-reaction of the cytochrome oxidase procedure with horseradish peroxidase, it was possible to trace many neurons through both series of sections. Middle tufted cells of the superficial EPL have basal dendrites confined to the superficial zone of light cytochrome oxidase staining. Internal tufted cells and middle tufted cells of the intermediate zone send their basal dendrites into the intermediate zone. One group of mitral cells (type I) has basal dendrites confined to the deep zone of lighter cytochrome oxidase staining. A second group of mitral cells (type II) and tufted cells of the intermediate EPL has basal dendrites primarily confined to the intermediate zone of dark cytochrome oxidase staining. The correlation of the enzyme staining with the dendritic laminar patterns supports the existence of three relatively distinct sublaminae in the EPL and supports the designation of two types of mitral cells. The staining pattern also provides an independent method for evaluating the sublaminae of the EPL without the necessity of labeling individual groups of cells. Finally, the staining pattern suggests that the intermediate zone of the EPL may be subjected to more tonic synaptic input, causing it to have an increased level of metabolic activity.

Animals↗
PubMed2005

Oxidase reaction of the hybrid Mn-peroxidase of the fungus Panus tigrinus 8/18.

The hybrid Mn-peroxidase of the fungus Panus tigrinus 8/18 oxidized NADH in the absence of hydrogen peroxide, this being accompanied by the consumption of oxygen. The reaction of NADH oxidation started after a period of induction and completely depended on the presence of Mn(II). The reaction was inhibited in the presence of catalase and superoxide dismutase. Oxidation of NADH by the enzyme or by manganese(III)acetate was accompanied by the production of hydrogen peroxide and superoxide radicals. In the presence of NADH, the enzyme was transformed into a catalytically inactive oxidized form (compound III), and the latter was inactivated with bleaching of the heme. The substrate of the hybrid Mn-peroxidase (Mn(II)) reduced compound III to yield the native form of the enzyme and prevented its inactivation. It is assumed that the hybrid Mn-peroxidase used the formed hydrogen peroxide in the usual peroxidase reaction to produce Mn(III), which was involved in the formation of hydrogen peroxide and thus accelerated the peroxidase reaction. The reaction of NADH oxidation is a peroxidase reaction and the consumption of oxygen is due to its interaction with the products of NADH oxidation. The role of Mn(II) in the oxidation of NADH consisted in the production of hydrogen peroxide and the protection of the enzyme from inactivation.

Catalase↗
PubMed1989

Coupled reactions for the determination of analytes and enzymes based on the use of luminescence.

Immobilized enzymes are widely used in the clinical laboratory in the assay of several analytes and enzymes. The use of immobilized enzymes makes these reagents recoverable and re-usable, and in most cases increases their stability and catalytic activity. In conjunction with bioluminescent enzymes (firefly and bacterial luciferases) and chemiluminescent catalyst (peroxidase) we set up high-sensitive flow methods based on the use of nylon tube coil or epoxy methacrylate column as solid support. All the NAD(P)/NAD(P)H-dependent dehydrogenases (bacterial luciferase), ATP-dependent enzymes (firefly luciferase) and oxidases producing H2O2 (peroxidase) can be immobilized and a large variety of analytes have been sensitively measured. As an alternative format we also reported a dry chemistry method in which all the enzymes, substrates and cofactors are ready to use, supported on dry cellulose disks. Methodological problems such as flow conditions, stability, pH, ionic strength and analytical performances are also reported.

Animals↗
PubMed2000

A homokaryotic derivative of a Phanerochaete chrysosporium strain and its use in genomic analysis of repetitive elements.

Analysis of complex gene families in the lignin-degrading basidiomycete Phanerochaete chrysosporium has been hampered by the dikaryotic nuclear condition. To facilitate genetic investigations in P. chrysosporium strain BKM-F-1767, we isolated a homokaryon from regenerated protoplasts. The nuclear condition was established by PCR amplification of five unlinked genes followed by probing with allele-specific oligonucleotides. Under standard nitrogen-limited culture conditions, lignin peroxidase, manganese peroxidase, and glyoxal oxidase activities of the homokaryon were equivalent to those of the parental dikaryon. We used the homokaryon to determine the genomic organization and to assess transcriptional effects of a family of repetitive elements. Previous studies had identified an insertional mutation, Pce1, within lignin peroxidase allele lipI2. The element resembled nonautonomous class II transposons and was present in multiple copies in strain BKM-F-1767. In the present study, three additional copies of the Pce1-like element were cloned and sequenced. The distribution of elements was nonrandom; all localized to the same 3.7-Mb chromosome, as assessed by segregation analysis and Southern blot analysis of the homokaryon. Reverse transcription-PCR (RT-PCR) showed that Pce1 was not spliced from the lipI2 transcript in either the homokaryon or the parental dikaryon. However, both strains had equivalent lignin peroxidase activity, suggesting that some lip genes may be redundant.

Chromosome Mapping↗
PubMed2005

Etiology of UV-C-induced browning in var. Superior white table grapes.

White table grapes, var. Superior, were treated with UV-C light after harvest to increase stilbenes concentration, especially trans-resveratrol (RES), because this may be of relevance to the health-promoting properties assigned to these compounds. However, irradiated grapes also developed some browning on the surface on the third day of storage at 22 degrees C, with the subsequent detriment in the sensorial quality of the fruit. Possible causes for browning development during storage were investigated. The phenolic-related oxidative enzymes, polyphenol oxidase (PPO) and peroxidase (POD), were not specifically activated, and no new isoforms appeared upon UV-C treatment. UV-treated grapes had lower content of chlorophyll b than control grapes on the fourth day of storage, concomitant with the increase of pheophytins (chlorophyll degradation derived compounds). Microscopy data showed lower fluorescence emission in chloroplasts from the UV-treated samples, which may explain the decrease of chlorophylls content in the corresponding grape berries extracts. In addition, microscopy images showed cell wall thickening in the skin tissue of UV-treated grapes which could be considered as a general wound response in plant tissues. These results suggest that the development of browning in Superior white grapes after UV-C treatment is not closely related with the evolution of oxidative enzymes during storage and may be mainly due to the decrease of chlorophylls content.

Catechol Oxidase↗