Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Acetaminophen, p-aminophenol, and oxyphenbutazone interfere with the glucose oxidase/peroxidase method for glucose. Structurally related compounds that lack a free phenolic hydroxyl group (acetanilide, aniline, and phenylbutazone) do not interfere. During the analytical procedure acetaminophen is consumed. One mole of acetaminophen leads to an apparent loss of four moles of glucose. The hexokinase/glucose-6-phosphate dehydrogenase method (Boehringer Hexokinase method) is not affected by these substances.
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PMID:Interference by acetaminophen in the glucose oxidase-peroxidase method for blood glucose determination. 97 21

Phenidone is not a substrate for dioxygenation by soybean lipoxygenase-1 (L1) but reduces L1Fe(III) into L1Fe(II), as shown by EPR spectroscopy. L1 catalyzes the oxidation of phenidone by 13-HPOD, the hydroperoxide formed by dioxygenation of linoleic acid by L1, with formation of 4,5-dehydrophenidone. Two moles of 13-HPOD are used per mole of phenidone dehydrogenated. Other pyrazoline derivatives such as BW 755C, but also, in a more general manner, different compounds containing phenol, aniline, hydrazine, hydroxylamine or hydrazide functions act as reducing substrates for decomposition of 13-HPOD by L1.
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PMID:Soybean lipoxygenase-catalyzed oxidations by linoleic acid hydroperoxide: different reducing substrates and dehydrogenation of phenidone and BW 755C. 312 36

The yeast Saccharomyces cerevisiae, produces a cytochrome P-450 enzyme with a Soret peak in the reduced-CO difference spectrum at 448 nm. The enzyme purified to homogeneity (88-97% pure on a specific content basis) has a molecular wt. of 55 500 as determined by SDS-PAGE. Amino acid analysis of yeast cytochrome P-448 revealed 407 amino acid residues per molecule with a 43% complement of hydrophobic residues. Although the number of residues is smaller than cytochrome P-448 enzymes from mammalian sources, the percentage of hydrophobic residues is almost identical. Estimation of the haem content of yeast cytochrome P-448 showed that one haem group was present per molecule. Phospholipid was present at very low levels. The molecular wt. of the polypeptide chain plus an estimated 5-6 units of hexose and of hexosamine is in good agreement with the molecular wt. value obtained from SDS-PAGE. A reconstituted system of purified cytochrome P-448, purified NADPH-cytochrome P-450 (c) reductase and phospholipid showed aryl hydrocarbon hydroxylase activity towards benzo[a]pyrene. Both protein components, NADPH and dilauroyl phosphatidylcholine (or emulgen 911) were necessary for full activity. The NADPH requirement could be replaced by cumene hydroperoxide or H2O2 generated in situ from a glucose oxidase system; in each case Vmax is increased, but the apparent affinity for benzo[a]pyrene, as measured by an increased Km, is lowered. The spin state of purified yeast cytochrome P-448 was 94% low spin (22 degrees C) as determined from the temperature-dependent spin-state equilibrium. The addition of benzo[a]pyrene to this enzyme resulted in a change to higher spin state (18% high spin at 22 degrees C). Equilibrium gel filtration analysis of the number of benzo[a]pyrene binding sites per mole of enzyme monomer showed a value of 1 for purified yeast cytochrome P-448 and 6 for this enzyme in microsomal form. The corresponding values for purified and microsomal cytochrome P-450 from phenobarbital-pretreated rats are 1 and 6, respectively. However, purified cytochrome P-448 from beta-naphthoflavone-induced rats gave a value of 6 benzo[a]pyrene binding sites. Type I binding spectra with purified yeast cytochrome P-448 were observed with benzo[a]pyrene, lanosterol, ethylmorphine, dimethylnitrosamine, sodium phenobarbitone and perhydrofluorene. Type II spectral changes were observed with imidazole, aniline and benzphetamine. Cytochrome P-448 from Saccharomyces cerevisiae is identified as a distinct enzyme of the P-450 family. This enzyme however has many properties in common with cytochrome P-448 from mammalian sources.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Studies on the properties of highly purified cytochrome P-448 and its dependent activity benzo[a]pyrene hydroxylase, from Saccharomyces cerevisiae. 632 93

Untreated monkey liver cytochrome P-450 (monkey P-450) has been purified to a specific content of 14.9 n mole/mg protein. The purified preparation was apparently homogeneous and the minimum molecular weight was estimated to be 50,000 by SDS-PAGE. Absolute spectrum of the oxidized form showed peaks at 565, 535 and 417 nm. The monkey P-450 was active in the mixed function oxidation of benzphetamine, aminopyrine, ethylmorphine, aniline and 7-ethoxycoumarin in the presence of rat liver NADPH-cytochrome P-450 reductase and DLPC. Anti monkey P-450 IgG could not inhibit rat P-450s (PB P-450, MC P-448(1) and MC P-448(2] catalyzed 7-ethoxycoumarin O-deethylation activities.
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PMID:Purification and properties of cytochrome P-450 from untreated monkey liver microsomes. 651 38

Thiaminase (EC 2.5.1.2) from freshwater bivalve molluscs is a polycosubstrate enzyme, which is resistant to temperatures below 55 degrees. The activation energy of the enzyme with cystein is 15077 cal/mole, with aniline--15948 cal/mole. Thiaminase when injected parenterally to albino mice 2 hrs after injection of [2-14C]thiamine causes an extensive destruction of labelled vitamin b1, which is evidenced from the [14C]thiazole content in urine, liver and kidneys. The total radioactivity and the content of [14C]thiazole in the urine samples collected within 6 hrs after thiamine injection are increased. Cysteine and histidine in combination with thiaminase have no activating effect similar to that observed "in vitro". In the experimental series when non-labelled vitamin B1 from animal tissues (liver, kidney, spleen, muscle) was substituted by the labelled one, the parenterally injected enzyme destroyed up to 30-50% of total thiamine content. Brain and skeletal muscle tissues are more resistant to thiaminase action.
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PMID:[Direct measurement of the antivitamin action of parenterally injected thiaminase]. 724 48

A laboratory study was conducted to determine whether tetryl (2,4,6-trinitrophenylmethylnitramine) can be degraded by an anaerobic process. The results indicated that the metabolic conversion of tetryl to aniline is possible by a sulfate-reducing bacterial (SRB) consortium. This SRB consortium metabolized tetryl by co-metabolism with pyruvate as a growth substrate. For every mole of tetryl metabolized, 1 mole of aniline was produced, and the aniline was further metabolized. This metabolic conversion of tetryl is likely to be of value in the anaerobic treatment of tetryl-contaminated soil and ground water, such as found at many military ammunition sites.
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PMID:Formation of aniline as a transient metabolite during the metabolism of tetryl by a sulfate-reducing bacterial consortium. 1067 52

The mechanism of oxidation or reduction using the electron method was investigated for (I) aniline; (II) nitrobenzene; (III) nitrate; (IV) sulphanilamide; (V) hydrogen peroxide; (VI) hydroxyl free radical; (VII) ferricyanide; (VIII) acetylphenylhydrazine; (IX) nitrite; (X) chlorate and (XI) hydroxylamine respectively. Substances (II), (III), (V), (VI), (VII), (IX), (X) and (XI) evolved as oxidants, with (II), nitrobenzene and (X), chlorate as the most powerful oxidants (number of moles of HbFe(2+)(haemoglobin) of 6 reacting with 1.0 mole of the substance). Substances (I), (IV) and (VII) evolved as reductants of equal reducing power (number of moles of HbFe(3+)(methaemoglobin) of 4 reacting with 1.0 mole of the substance). Using the following equations, the impact of oxidants and reductants on glutathione (GSH) peroxidase, glutathione (GSSC) reductase and NADHmetHb reductase respectively on methaemoglobinaemia generation was investigated. [Equation in text]. Redox potential change (DeltaE' (o)) of 1.77, -1.77 and 1.86 volt and free energy change (DeltaG(o)') of -81, 81 and -85.8 kcal/mol were calculated for GSH peroxidase, GSSG reductase and NADHmetHb reductase systems respectively. In sustained methaemoglobinaemia, these mechanisms predict low levels of NADHmetHb reductase and glutathione peroxidase respectively, but high levels of glutathione reductase in red blood cells on exposure to oxidants. The significance of these mechanisms was investigated in cord blood, neonatal, adult red blood cells and other biological systems. It was concluded that any reaction with a positive DeltaE(o)' and negative DeltaG(o)' with the Fe(3+): Fe(2+)couple will indicate methaemoglobin oxidizing power. The effects on red blood cells and white blood cells were manifested in the biochemical toxicology of nitroso (PhN = 0), arylamine glucuronide (PhNHG) and arene imine respectively.
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PMID:Theoretical mechanistic basis of oxidants of methaemoglobin formation. 1079 Jul 68

We demonstrate here, for the first time, a unique strategy for conducting polyaniline nanofibers based on renewable resources. Naturally available cardanol, which is an industrial waste and main pollutant from the cashew nut industry, is utilized for producing well-defined polyaniline nanofibers. A new amphiphilic molecule is designed and developed from cardanol, which forms a stable emulsion with aniline for a wide composition range in water (1:1 to 1:100 dopant/aniline mole ratio) to produce polyaniline nanofibers. The scanning electron microscopy and transmission electron microscopy analysis of the nanofibers reveals that the dopant/aniline ratio plays a major role in determining the shape and size of polyaniline nanofibers. The nanofiber length increases with the increase in the dopant/aniline ratio, and perfectly linear, well-defined nanofibers of lengths as long as 7-8 muM were produced. The amphiphilic dopant has a built-in head-to-tail geometry and effectively penetrates into the polyaniline chains to form highly organized nanofibers. Wide-angle X-ray diffraction (WXRD) spectra of the nanofibers showed a new peak at 2theta = 6.3 (d spacing = 13.9 A) corresponding to the three-dimensional solid-state ordering of polyaniline-dopant chains, and this peak intensity increases with increase in the nanofiber length. The comparison of morphology and WXRD reveals that high ordering in polyaniline chains results in the formation of long, well-defined nanofibers, and this direct correlation for the polyaniline nanofibers with solid-state ordering has been established. The conductivity of the polyaniline nanofibers also increases with increase in the solid-state ordering rather than increasing with the extent of doping. The polyaniline nanofibers are freely soluble in water and possess high environmental and thermal stability up to 300 degrees C for various applications.
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PMID:New renewable resource amphiphilic molecular design for size-controlled and highly ordered polyaniline nanofibers. 1676 35

The thermal decomposition of anthranil diluted in argon was studied behind reflected shock waves in a 2 in. i.d. pressurized driver single-pulse shock tube over the temperature range 825-1000 K and overall densities of approximately 3 x 10(-5) mol/cm(3). Two major products: aniline and cyclopentadiene carbonitrile (accompanied by carbon monoxide) and four minor products resulting from the decomposition were found in the postshock samples. They were, in order of decreasing abundance, pyridine, CH(2)=CHCN, HCN and CHC-CN, and comprised only a few percents of the overall product distribution. Quantum chemical calculations were carried out to determine the sequence of the unimolecular reactions that lead to the formation of cyclopentadiene carbonitrile and of phenylnitrene/phenylimine that are the precursors of aniline. They form aniline by reactions with traces of water impurities. To produce cyclopentadiene carbonitrile, two main processes must take place: CO elimination and ring contraction from a six- to a five-membered ring. It was shown that this can occur via two parallel pathways where CO elimination takes place prior to or following ring contraction. Singlet potential energy surfaces for all the elementary reactions that lead to the formation of cyclopentadiene carbonitrile and phenylnitrene/phenylimine were obtained. Their rate constants were calculated on the basis of the results of the quantum chemical calculations using transition-state theory. A kinetic scheme containing these reactions was constructed and multiwell calculations were performed to evaluate the mole percent of the products as a function of temperature. A very serious disagreement between the experimental results and the results of calculations showed that the singlet PESs could not account for the observed experimental rates. No other singlet PESs that lead to the formation of these products could be found. In view of this observation, attempts to find pathways that lead to the formation of cyclopentadiene carbonitrile and phenylnitrene/phenylimine on triplet surfaces were made. Such surfaces were found, and singlet <--> triplet intersystem crossing probabilities and crossing rate constants were calculated as well as the rate constants of all the elementary steps on the triplet surfaces. A reaction scheme was constructed and multiwell calculations were performed, including also the pathways on the singlet surfaces, to evaluate the mole percent of the products as a function of temperature. The agreement between the experimental results and these calculations was quite satisfactory.
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PMID:Decomposition of anthranil. Single pulse shock-tube experiments, potential energy surfaces and multiwell transition-state calculations. The role of intersystem crossing. 1682 8

The effect of solvent participation on the ligand-to-metal charge transfer (LMCT, L-->Co(III)) reduction of the of Co(III)(en)(2)Br(RC(6)H(4)NH(2))(2+) where R=m-OCH(3), p-F, H, m-CH(3), p-CH(3,)p-OC(2)H(5) and p-OCH(3) were examined in aqueous 2-methyl-2-propanol (Bu(t)OH) solutions. The change in the reduction behavior of Co(III) centre was also examined through cyclic voltammetric studies. The observed reduction in quantum yield due to LMCT excitation can mainly be accounted using linear solvation energy relationship (LSER) comprising model correlation equations. These consist of empirical parameters such as Grunwald-Winstein's solvent ionizing power, Y, Dimroth-Richardt's solvent micro-polarity parameter, E(T)(N), Gutmann's donor number, DN(N), along with Kamlet-Taft's solvatochromic parameters (hydrogen bond acceptor acidity/basicity alpha/beta and solvent dipolarity/polarizability, pi*). The origin of solvent effect is found to be due to microscopic interaction between the solvent donor and the nitrogen-bound hydrogen of the ligand. Cyclic voltammograms show an irreversible reduction of Co(III) in DMF using Glassy Carbon Electrode, GCE, the redox peaks for the aniline complexes appear at -0.20 and 0.525V. Irradiation of the complexes with UV light (lambda=254nm) in binary mixtures produce Co(II)(aq) and the concentration of this species are highly dependent on x(alc) (x(alc)=mole fraction of alcohol). The observed quantum yield (logPhi(Co(II))) is found to be linearly related to mole fraction of organic co-solvent added in the mixture, therefore, logPhi(Co(II))=26.41 x 10(-2) when x(2)=0.0094 and 43.75 x 10(-2) when x(2)=0.076 for a typical complex Co(III)(en)(2)Br(p-OCH(3)C(6)H(4)NH(2))(2+) in aqueous 2-methyl-2-propanol at 300K. Cyclic voltammetry and LSER analyses illustrate the variation of reduction property of Co(III) by the aryl ligand and homogeneous solvation of the excited state of the complex Co(III)(en)(2)Br(RC(6)H(4)NH(2))(2+) in H(2)O/Bu(t)OH mixtures.
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PMID:Homogeneous solvation controlled photoreduction of cobalt(III) complexes in aqueous 2-methyl-2-propanol solutions linear solvation energy relationship and cyclic voltammetric analyses. 1769 8


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