Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Pyrogallol”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 451 records · Page 25Linked to original sources

Inhibitory effects of phenolics, teas and saliva on the formation of mutagenic nitrosation products of salted fish.

The objectives of this study were to simulate in vitro some of the conditions that may prevail in man during the ingestion of a meal and to quantitate the inhibitory effect of phenolics and phenolic-containing beverages on the formation of mutagenic nitrosation products. The test system consisted of nitrosating (pH 2, 1 h, 37 degrees C) an aqueous fraction of a salt-preserved Chinese fish (Pak Wik) with or without the inhibitors to be tested and estimating the frequency of his+ revertants per survivor of Salmonella typhimurium (strain TA1535). The phenolics and teas were added to the nitrosation mixture. Catechin, chlorogenic acid, gallic acid, pyrogallol and tannic acid suppressed the formation of mutagenic nitrosation products. The inhibitory efficiency was comparable to that of ascorbic acid. A Japanese, a Chinese and a Ceylonese tea also prevented the formation of mutagenic nitrosated fish products at doses which are usually consumed by man. Moreover, saliva exerted an inhibitory effect. The inhibitory effect was not additive when the phenolics or saliva were added concurrently to the nitrosation mixture. The possibility that phenolics are involved in the apparent chemopreventive effect of fruits and vegetables is discussed.

Animals↗

Peroxidase, an alternate pathway to cytochrome P-450 for xenobiotic metabolism in skin: partial purification and properties of the enzyme from neonatal rat skin.

Peroxidase activity was partially purified from neonatal (3 to 6 days old) rat skin. The membrane-bound peroxidase activity was extracted with 0.5 M calcium chloride and was monitored spectrophotometrically at 470 nm with 2-methoxyphenol (guaiacol) and hydrogen peroxide as substrates. Subcellular distribution studies indicated the activity to be highest and comparable in nuclei and mitochondria, lowest in microsomes, and absent in cytosol. The peroxidase activity was partially purified by affinity chromatography on concanavalin A-sepharose 4B and by gel filtration using Bio-Gel P-150. Purification factors from these two steps were about 25 and 4, respectively. Peroxidase extraction in the presence of 2 mM N-ethylmaleimide increased activity about twofold. The combination of 2 mM N-ethylmaleimide and 10% (w/v) glycerol was found to be optimal for preservation of activity. Peroxidase activity increased linearly with increases in protein concentration, time, and guaiacol concentration. Activity was inhibited approximately 75% by 0.1 mM potassium cyanide or 0.05 mM sodium azide. Pyrogallol, hydroquinone, p-cresol, catechol, benzidine, 3,3'-dimethoxybenzidine, tetramethylbenzidine and p-phenylenediamine also acted as substrates for the rat cutaneous peroxidase.

Animals↗

Superoxide dismutase activities of spermatozoa and seminal plasma are not correlated with male infertility.

Abnormal reactive oxygen species (ROS) production is associated with defective sperm function. Superoxide dismutase (SOD) is related with the scavenging of seminal ROS. We aimed to determine the effect of SOD activities of spermatozoa and seminal plasma on sperm quality. Semen samples from infertile couples who consented to the analyses were divided into two groups: 1) normospermia (n = 20); and 2) oligoasthenozoospermia (n = 31). The SOD activities of the spermatozoa and seminal plasma were measured by determining the inhibition of pyrogallol autoxidation. The SOD activities of spermatozoa and seminal plasma in both groups were compared. The relationships between the SOD activities and the sperm qualities were determined. We noted that SOD activities of sperm/seminal plasma in both groups were nonsignificantly different (group 1 vs. 2 = 0.77 +/- 0.33/0.84 +/- 0.40 U/mg protein for sperm, and 0.66 +/- and 0.36/0.83 +/- 0.47 U/ml for seminal plasma). SOD activities of sperm/seminal plasma were positively but nonsignificantly correlated with the sperm motility (SOD of sperm = 0.0008 x motility + 0.67; SOD of seminal plasma = 0.0006 x motility + 0.81) and concentration (SOD of sperm = 0.0006 x concentration + 0.67; SOD of seminal plasma = 0.0021 x concentration + 0.73). We concluded that SOD activities of sperm and seminal plasma were nonsignificantly correlated with the seminal quality. It appears that the SOD survey is not a useful tool for determining sperm fertilization potential.

Antioxidants↗

Biodegradation of gallotannins and ellagitannins.

Nowadays, many researches have been made on gallotannin biodegradation and have gained great success in further utilization. Some of industrial applications of these findings are in the production of tannase, the biotransformation of tannic acid to gallic acid or pyrogallol and detannification of food and fodder. Although ellagitannins have the typical C-C bound which is more difficult to be degraded than gallotannins, concerted efforts are still in progress to improve ellagitannin degradation and utilization. Currently, more attention is mainly focused on intestinal microflora biodegradation of tannins especially ellagitannins which can contribute to the definition of their bioavailability for both human beings and ruminants. Also there have been endeavours to utilize the tannin-degrading activity of different fungi for ellagitannin-rich biomass, which will facilitate application of tannin-degrading enzymes in strategies for improving industrial and livestock production. Due to the complicated structures of complex tannins and condensed tannins, the biodegradation of them is much more difficult and there are fewer researches on them. Therefore, the researches on the mechanisms of gallotannin and ellagitannin biodegradation can result in the overall understanding to the biodegradation of complex tannins and condensed tannins. Biodegradation of tannins is in an incipient stage and further studies have to be carried out to exploit the potential of various tannins for largescale applications in food, fodder, medicine and tannery effluent treatment.

Animals↗

Utilization of aromatic compounds by the Penicillium strain Bi 7/2.

The Penicillium strain Bi 7/2 utilized phenol, catechol, resorcinol, hydroquinone, pyrogallol, hydroxyhydroquinone, phloroglucinol, m- and p-cresol, orcinol, 4-methylcatechol, 4-methoxyphenol, 4-aminophenol, benzyl alcohol, benzoic acid, 2-, 3- and 4-hydroxybenzoic acid, anthranilic acid, protocatechuic acid and gallic acid as sole sources of carbon and energy. The central metabolites catechol, protocatechuic acid and hydroxyquinone could be determined by HPLC with diode-array detection. Pathways for the degradation of aromatic substances were proposed.

Biodegradation, Environmental↗

Phenol degradation by Acinetobacter calcoaceticus NCIB 8250.

Acinetobacter calcoaceticus NCIB 8250 utilizes phenol as sole source of carbon and energy via an ortho-cleavage pathway. The presence of ethanol in mixed substrate cultivations repressed the utilization of phenol. In fed batch cultivation the phenol tolerance was increased at least 2-fold. Maximum degradation rates of 150 mg phenol/(1 h) and 280 mg phenol/(g h), respectively were observed. Phenol hydroxylase is induced by its substrate and in parallel the catechol-1,2-dioxygenase is detectable. The presence of active phenol hydroxylase is strongly connected with the phenol degradation. Using a spectrophotometric enzyme assay the partially purified phenol hydroxylase was characterized with respect to kinetic parameters. The apparent Km values for phenol, FAD and NADPH were estimated to be 147 microM, 35 microM and 416 microM, respectively. Both FAD and NADPH were essential for maximum activity of the cytoplasmically localized enzyme. No substrate inhibition of phenol hydroxylase by phenol was observed up to 0.8 mM. The pH and temperature optima were pH 7.8 and 33 degrees C, respectively. The partially purified enzyme showed a broad substrate specificity. It hydroxylated the three isomeric cresols, chlorophenols and methylated chlorophenols. Pyrogallol, 3,4-dihydroxy-L-phenylalanine and resorcinol were oxygenated with higher rates than phenol. With the exception of phenol all other enzyme substrates tested did not serve as growth substrates.

Acinetobacter calcoaceticus↗

Antioxidant efficiency of polyhydric phenols in photooxidation of benzaldehyde.

An experimental system is described for the observation of the kinetics of photochemically initiated oxidation reactions; this system is based on the measurement of oxygen consumption with a polarographic oxygen electrode. The photooxidation of benzaldehyde in dilute aqueous solution was examined and appears to conform to a free radical chain mechanism. The antioxidant efficiency of some polyhydric phenols was determined kinetically and found to be catechol greather than pyrogallol greater than hydroquinone greather than resorcinol greater than n-propyl gallate for the benzaldehyde photooxidation.

Antioxidants↗

Ca2+ activation of wheat peroxidase: a possible physiological mechanism of control.

Peroxidation of substrates such as ascorbic acid, pyrogallol, or ferulic acid, as well as indole acetic acid oxidation catalyzed by wheat germ peroxidase (WGP)2 C2, were found to be activated by Ca2+. This activation is independent of the stabilizing effect of structural Ca2+ reported for peroxidases. Steady state kinetics of ferulic acid oxidation catalyzed by WGP C2 showed an increase in the rate of compound I formation and of compound II decomposition in the presence of the ion, evidenced as an increase in rate constants k1, from 8.9 x 10(5) to 4.5 x 10(5) M-1 cm-1, and k3, from 4.4 x 10(5) to 1.1 x 10(6) M-1 cm-1. The dissociation constant Kd, for the cyanide derivative of the enzyme showed a marked decrease from 220 to 34 microM in the presence of Ca2+, thus implying an effect of the ion in the H2O2 binding step. In the presence of Ca2+, a conformational change in the protein was revealed by tryptophan fluorescence, providing a basis for the activation mechanism. Other peroxidases such as horseradish peroxidase and WGP C3 were not activated by Ca2+. The results suggest the existence of a physiological mechanism of control of peroxidase isozymes activity mediated by Ca2+.

Calcium↗

Electron paramagnetic resonance studies of radical species of proanthocyanidins and gallate esters.

The polyphenols present in green tea or red wine comprise both regular flavon(ol)s and proanthocyanidins, i.e., derivatives of flavan-3-ols, whose distinct antioxidative potential is of great importance for explaining the beneficial effects of these nutrient beverages. Using EPR spectroscopy, we investigated radical structures obtained after oxidation of the parent compounds either by horseradish peroxidase/hydrogen peroxide or after autoxidation in moderately alkaline solutions. Both proanthocyanidins (monomers of condensed tannins, e.g., (+)-catechin, (-)-epicatechin, (-)-epicatechin gallate, (-)-epigallocatechin, (-)-epigallocatechin gallate, Pycnogenol) and gallate esters (hydrolyzable tannins, e.g., propylgallate, beta-glucogallin, pentagalloyl glucose and tannic acid) yielded predominantly semiquinone structures derived from the parent catechol or pyrogallol moieties. Evidence for a time-dependent oligomerization was obtained for (-)-epigallocatechin gallate, supporting our hypothesis that o-quinones formed from the initial semiquinone disproportionation are prone to nucleophilic addition reactions. Such phenolic coupling reactions would retain the numbers of reactive catechol/pyrogallol structures and thus the antioxidative potential. We therefore propose that proanthocyanidins are superior antioxidants as compared to flavon(ol)s proper, whose quinones are more likely to redox-cycle and act as prooxidants.

Anthocyanins↗

A liquid chromatographic method for the simultaneous determination of alpha-tocopherol and tocopherolquinone in human red blood cells and other biological samples where tocopherol is easily oxidized during sample treatment.

A liquid chromatographic method for the simultaneous determination of alpha-tocopherol and tocopherolquinone in human red blood cells is described. Tocopherols in the red cell membrane are very susceptible to oxidation during sample processing. Red cell samples are saponified in the presence of a mixture of butylated hydroxytoluene, ascorbic acid, and pyrogallol and then extracted with hexane. The tocopherol compounds are separated on a C-18 column using a mobile phase containing 12% acetonitrile, 83% methanol, and 5% buffer (NaH2PO4.H2O, 7.5 mM final concentration) and are detected electrochemically. The mixture of antioxidants is essential to avoid loss of the tocopherol compounds during processing of samples. The use of acetonitrile in the mobile phase results in the separation of tocopherolquinone from delta-tocopherol. The proposed method may be generally suitable for the analysis of biological samples where tocopherols are especially vulnerable to oxidation. The levels of tocopherolquinone and delta-tocopherol in normal red cells are quite small (less than 1% of alpha-tocopherol). The ratio of tocopherol and tocopherolquinone concentrations might serve as a useful index of the redox status of red cell membranes, particularly under in vitro conditions.

Biological Assay↗

NO- and NO2-carrying molecules potentiate photorelaxation in rat trachea and aorta.

Photorelaxation elicited by ultraviolet light (366 nm) was investigated on isolated rat thoracic aorta and trachealis. Rat tracheal smooth muscle but not aorta did not show UV-induced photorelaxation. Both streptozotocin, NO-carrying molecule and N omega-nitro-L-arginine, NO2-carrying molecule significantly enhanced photorelaxation, concentration-dependently, in rat trachealis and aorta. Methylene blue (10 microM) inhibited the potentiation action of streptozotocin and N omega-nitro-L-arginine in both tissues. Superoxide dismutase (300 U/ml) enhanced streptozotocin- and N omega-nitro-L-arginine-potentiated photorelaxation in rat trachealis, while pyrogallol (0.1 mM), a potent O2- generating agent, inhibited streptozotocin-potentiated photorelaxation in trachealis. Streptozotocin was much more effective than N omega-nitro-L-Arginine in potentiating of photorelaxation elicited by UV light in both tissues. From these findings, we conclude that streptozotocin and N omega-nitro-L-arginine produce EDRF like labile substance(s) by UV irradiation.

Animals↗

Preparation and initial characterization of the compound I, II, and III states of iron methylchlorin-reconstituted horseradish peroxidase and myoglobin: models for key intermediates in iron chlorin enzymes.

To better understand the spectral properties of high valent and oxyferrous states in naturally occurring iron chlorin-containing proteins, we have prepared the oxoferryl compound I derivative of iron methylchlorin-reconstituted horseradish peroxidase (MeChl-HRP) and the compound II and oxyferrous compound III states of iron MeChl-reconstituted myoglobin. Initial spectral characterization has been carried out with UV-visible absorption and magnetic circular dichroism. In addition, the peroxidase activity of iron MeChl-HRP in pyrogallol oxidation has been found to be 40% of the rate for native HRP. Previous studies of oxoferryl chlorins have employed tetraphenylchlorins in organic solvents at low temperatures; stable oxyferrous chlorins have not been previously examined. The present study describes the compound I, II, and III states of histidine-ligated iron chlorins in a protein environment for the first time.

Animals↗

Scavenging of peroxynitrite by phycocyanin and phycocyanobilin from Spirulina platensis: protection against oxidative damage to DNA.

Peroxynitrite (ONOO(-)) is known to inactivate important cellular targets and also mediate oxidative damage in DNA. The present study has demonstrated that phycocyanin, a biliprotein from spirulina platensis and its chromophore, phycocyanobilin (PCB), efficiently scavenge ONOO(-), a potent physiological inorganic toxin. Scavenging of ONOO(-) by phycocyanin and PCB was established by studying their interaction with ONOO(-) and quantified by using competition kinetics of pyrogallol red bleaching assay. The relative antioxidant ratio and IC(50) value clearly indicate that phycocyanin is a more efficient ONOO(-) scavenger than PCB. The present study has also shown that PCB significantly inhibits the ONOO(-)-mediated single-strand breaks in supercoiled plasmid DNA in a dose-dependent manner with an IC(50) value of 2.9 +/- 0.6 microM. These results suggest that phycocyanin, has the ability to inhibit the ONOO(-)-mediated deleterious biological effects and hence has the potential to be used as a therapeutic agent.

Cyanobacteria↗

Effects of inflammation on copper antioxidant enzyme levels.

Inflammation increases plasma levels of ceruloplasmin, a copper protein with possible antioxidant function. This paper describes modulation of these increases by copper intake, and describes combined effects of inflammation and copper intake on Cu-Zn and extracellular (EC) superoxide dismutase (SOD) activities. Turpentine injections in rats fed 1 of 4 copper levels increased ceruloplasmin activities, but values were sensitively limited by copper intake. Cu-Zn SOD activities in the liver, but not in erythrocytes or lungs, were reduced by inflammation in each dietary copper group. Inflammation in rats fed a standard mixed feed diet reduced plasma EC superoxide dismutase activities measured by inhibition of pyrogallol autoxidation. Different results were obtained with 3 xanthine oxidase based SOD assays which were each subject to assay interference. Studies in humans found a group of rheumatoid arthritis patients to possess relatively low erythrocyte SOD and relatively high ceruloplasmin activities. Activity levels of SOD, but not of ceruloplasmin, increased after 4 weeks of copper supplementation (2 mg/day). The fate of cellular Cu-Zn SOD activity contents in inflamed tissues is largely uninvestigated. However, interleukin-1, a hormone released at inflammation sites, elevated Cu-Zn SOD activities in cultured fibroblasts.

Animals↗

The significance of free radicals and free radical scavengers in L1210 leukemia.

L1210 leukemia is a murine leukemia which is associated with anemia and marked neutrophilia. In order to determine the significance of free radicals (FR) in this disorder, we determined the presence and localization of free radical scavengers (FRS) and scavenger-like systems in L1210 leukemia cells obtained in vivo and from in vitro cultures. FR are metabolized or detoxified by certain FRS such as glutathione (GSH and GSSG), superoxide dismutase (SOD) and enzymes such as epoxide hydrolase (EH). In all cases specific fractions of L1210 cells, bone marrow and liver were examined for FR/FRS levels. Reduced (GSH) and oxidized (GSSG) glutathione were measured fluorometerically using o-opthalaldehyde (OPT). SOD was determined colorimetrically utilizing pyrogallol by substrate autolysis inhibition, and EH was determined by utilizing [3H] styrene oxide as a substrate. Ratios of GSH/GSSG in fractions prepared from in vivo and in vitro L1210 cells showed a predominance of GSH-reductase with the highest activity in mitochondria (ratio = 15 vs. 10). Normal liver showed a similar pattern whereas, leukemic liver showed altered GSH/GSSG ratios in mitochrondria and microsomes. Leukemic bone marrow showed a predominance of GSH-reductase in all fractions. EH activity was highest in microsomal fractions obtained from L1210 cells grown in vitro and found to become increased in both the mitrochondrial (100%) and microsomal (200%) fractions when cells were exposed to retinoic acid (RA) in culture. SOD activity in the cytosolic (21.2 U SOD/mg) and mitochondrial (12 U SOD/mg) fractions whereas, leukemic liver showed a significant decrease in activity in all fractions compared to normals. SOD was determined in fractions taken from L1210 cells in vivo and in vitro. Results demonstrated detectable but reduced SOD activity in the L1210 cell fractions as contrasted with liver activity. Results from these studies indicate that certain FRS systems are functional in L1210 leukemic animals. Furthermore, variations in the ratios or levels may be of significance in the leukemic and hematological states.

Animals↗

Comparative inhibition of enzymes of human erythrocytes and plasma in vitro by agricultural chemicals.

Farm workers generally are exposed to a combination of synthetic agricultural chemicals and natural products while working in the fields. These biologically active compounds control infestation of tobacco by insects, and plant growth. We have investigated, in vitro, the effects of acephate (AP), cadmium (Cd), methamidophos (MAP), maleic hydrazide (MH), and nicotine (NI) on the activities of the erythrocyte enzymes delta-aminolevulinic acid dehydratase (ALAD), superoxide dismutase (SOD), and plasma cholinesterase (CHE). ALAD, SOD, and plasma CHE were assayed, using aminolevulinic acid, pyrogallol, or butyryl thiocholine as substrates, respectively. Different concentrations of the above chemicals were used to obtain minimum and maximum inhibition of the enzymes, and for the development of inhibition dose response curves. These curves were used to determine the concentration of each chemical required to inhibit 50% of enzyme activity (I50). The I50 concentrations of various chemicals for each enzyme were determined in mM for ALAD: AP=95.5, Cd=1.4x10(-3), MH=2.8, MAP=7.1, NI=60.8; for SOD: AP=1.2, Cd=0.8x10(-7), MH=0.04, MAP=0.42, NI=0.81; for CHE: AP=5.6, Cd=18. 8x10(-5), MAP=18.4x10(-4); CHE was not inhibited by MH and NI. Our data indicate that AP inhibited both SOD and CHE to a maximum of 91 and 87%, while MH inhibited both SOD and ALAD to a maximum 78 and 90%. However, SOD was the enzyme that was most sensitive to all the agricultural-chemicals tested in this study. The inhibition of these enzymes will enable the development of a sensitive biomarker and the assessment of long term health risks in farm workers.

Agrochemicals↗

Holophaga foetida gen. nov., sp. nov., a new, homoacetogenic bacterium degrading methoxylated aromatic compounds.

A polyphasic approach was used in which genotypic and phenotypic properties of a gram-negative, obligately anaerobic, rod-shaped bacterium isolated from a black anoxic freshwater mud sample were determined. Based on these results, the name Holophaga foetida gen. nov., sp. nov. is proposed. This microorganism produced dimethylsulfide and methanethiol during growth on trimethoxybenzoate or syringate. The only other compounds utilized were pyruvate and trihydroxybenzenes such as gallate, phloroglucinol, or pyrogallol. The aromatic compounds were degraded to acetate. Although comparison of the signature nucleotide pattern of the five established subclasses of Proteobacteria with the 16S rDNA sequence of Holophaga foetida revealed a relationship to members of the delta-subclass, the phylogenetic position within the radiation of this class is so deep and dependent upon the number and selection of reference sequences that its affiliation to the Proteobacteria must be considered tentative. The type strain is H. foetida strain TMBS4 (DSM 6591).

Acetates↗

Possible physiological significance of the initial step in the catabolism of noradrenaline in the central nervous system of the rat.

The hypothalamus, the cerebral cortex and the cerebellar cortex of the rat were labelled in vitro with 3H-noradrenaline (3H-NA) and the metabolism of the tritiated transmitter was studied during spontaneous outflow and under conditions of release elicited by exposure to 20 mM K+. In the three areas of the central nervous system of the rat 3H-NA accounted for approximately 40% of the total radioactivity in spontaneous outflow while the 3H-O-methylated deaminated fraction (3H-OMDA) and 3H-3,4-dihydroxyphenylglycol (3H-DOPEG) were the main metabolites. Exposure to the reserpine-like agent, Ro 4-1284 induced a selective increase in the spontaneous outflow of 3H-DOPEG, while the contribution of the 3H-OMDA metabolites to the release induced by Ro 4-1284 was very small. During 3H-transmitter release elicited by exposure to 20 mM K+, approximately 80% of the radioactivity was collected as unmetabolized 3H-NA, while 3H-DOPEG was the main metabolite formed under these experimental conditions. Exposure to cocaine prevented 3H-DOPEG formation from 3H-NA released by K+, indicating that 3H-DOPEG was formed after neuronal reuptake of the transmitter released by K+. After in vitro labelling with 3H-NA, the unmetabolized transmitter represented approximately 70% of the total radioactivity retained in the tissue. However, when 3H-NA was administered in vivo, by intraventricular injection, only 30% of the total radioactivity retained by the tissue was accounted for by 3H-NA, and 60% of the radioactivity corresponded to the 3H-OMDA fraction, most of which was retained as 3H-MOPEG sulfate. When the rats were pretreated with pyrogallol, free 3H-DOPEG accounted for nearly 50% of the radioactivity retained in the three areas of the central nervous system after in vivo labelling with 3H-NA. When monoamine oxidase was inhibited by pargyline and 3H-NA was administered by intraventricular injection, 3H-NMN accounted for approximately 50% of the total radioactivity retained in the three areas of the central nervous system of the rat. The results obtained are compatible with the view that formation of the deamined glycol is the first step in the metabolism of 3H-NA in the rat central nervous system. In addition, it is concluded that the determination of the levels of some NA metabolites retained in the central nervous system does not necessarily represent an accurate reflection of the degree of central noradrenergic activity or of selective metabolic pathways. Consequently, in studies on the metabolism of NA it is important to take into account not only the transmitter and its metabolites in the tissue but also in the outflow from the structures studied either under in vivo or in vitro conditions.

2H-Benzo(a)quinolizin-2-ol, 2-Ethyl-1,3,4,6,7,11b-↗