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)

The enzyme preparation of L(+)-lactatoxydase (K.F. 1.1.3.2) with molecular weight of 230 000 has been isolated from the soluble fraction of the C. lipolytica cells and purified similar 360 times. The enzyme oxydizes L(+)-lactate, the optimum activity of the enzyme being observed at pH 8.0. Oxydation of the substrate is followed by accumulation of H2O2. Silver ions, p-chloromercurybenzoate and dicumarol inhibit the activity of L(+)-lactatoxydase. Iron complexones, cyanide and L-malate do not inhibit oxydation of the substrate. Pyruvate and its fluorine derivative practically do not produce any inhibiting effects either. The enzyme preparation contains 0.6 moles of flavin and 2 moles of nonhaem iron per a mole of the enzyme. Km value for the substrate is equal to 4-10(-4) M, Vmax--4.5 mkatom O/min/mg. Acidation of incubation medium leads to a decrease both of Km and Vmax. Km value for oxygen is equal to 3.1 mkM O2. Beside oxygen, ferricyanide, 2.6-dichlorphenolindophenol, phenazine methosulphate and cytochrome C may also serve as acceptors of L(+)-lactatoxydase electrons. The oxydized enzyme preparation is characterized by a spectrum absorption maximum at 410 nm. Upon L(+)-lactatoxydase reduction the maximum is shifted up to 420 nm.
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PMID:[Isolation and properties of cytoplasmic L(+)-lactatoxydase of Candida lipolytica yeasts]. 1 33

Trifluoroalanine is a mechanism-based inactivator of Escherichia coli tryptophan indole-lyase (tryptophanase) and E. coli tryptophan synthase (R. B. Silverman and R. H. Abeles, 1976, Biochemistry 15, 4718-4723). We have found that indole is able to prevent inactivation of tryptophan indole-lyase by trifluoroalanine. The protection of tryptophan indole-lyase by indole exhibits saturation kinetics, with a KD of 0.03 mM, which is comparable to the KI for inhibition of pyruvate ion formation (0.01 mM) and the Km for L-tryptophan synthesis. Fluoride electrode measurements indicate the formation of 28 mol of fluoride ion per mole of enzyme during inactivation of tryptophan indole-lyase, and 121 mol of fluoride ion are formed per mole of enzyme in the presence of 2 mM indole during the same incubation period. 19F NMR spectra of reaction mixtures of tryptophan indole-lyase and trifluoroalanine showed evidence only for fluoride ion formation, in either the absence or the presence of indole, and difluoropyruvic acid was not detected. The partition ratio, kcat/kinact, is estimated to be 9. Tryptophan indole-lyase in the presence of trifluoroalanine exhibits visible absorption peaks at 446 and 478 nm, which decay at the same rate as inactivation. However, in the presence of 1 mM indole and trifluoralanine, tryptophan indole-lyase exhibits a peak only at 420 nm, and the spectra show a gradual increase at 300-310 nm with incubation. In contrast, tryptophan synthase is not protected by indole from inactivation by trifluoroalanine, and the absorption peak at 408 nm for the tryptophan synthase-trifluoroalanine complex is unaffected by indole. These results demonstrate that inactivation of tryptophan indole-lyase occurs via a catalytically competent species, probably the beta,beta-difluoro-alpha-aminoacrylate intermediate, which can be partitioned from inactivation to products by a reactive aromatic nucleophile, indole.
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PMID:Indole protects tryptophan indole-lyase, but not tryptophan synthase, from inactivation by trifluoroalanine. 163 41

Projections from the medial (MSO) and lateral (LSO) superior olivary nuclei to the inferior colliculus (IC) were examined in the mole. In each mole, Fluoro-Gold was injected into one IC and wheat germ-agglutinated horseradish peroxidase (WGA-HRP) into the other IC; most MSO neurons were double-labeled bilaterally, while most LSO neurons were single-labeled bilaterally. The results indicate that the bilateral projections from the MSO and LSO to the IC are mainly established by single MSO neurons with axon collaterals to the IC on both sides, and by two separate populations of LSO neurons with axons to the contralateral or ipsilateral IC.
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PMID:Differential organization of crossed and uncrossed projections from the superior olive to the inferior colliculus in the mole. 170 16

To study the relationship between the exchangeable GTP binding site (E-site) and the high affinity metal binding site we synthesized P3-fluoro P1-5'-guanosine tripaosphate (GTP(gamma F), an analog of GTP. Our results show that this analog binds to the exchangeable GTP binding site of calf brain tubulin. The values of the dissociation constant and the stoichiometry of the GTP(gamma F)-Mn(II) complex as determined by EPR spectroscopy were 1.64 x 10(-4) M and one mole of manganese per mole of nucleotide, respectively. The distance separating the high-affinity binding site for the divalent metal ion and the exchangeable nucleotide binding site was evaluated by using high-resolution 19F-NMR. The 31P- and 19F-NMR spectra of GTP(gamma F) were studied, both the fluorine and the gamma-phosphate were split in a doublet with a coupling constant of 936 Hz. Tubulin purified by the method of Weisenberg (Weisenberg, R.C., and Timashef, S.N. (1970) Biochemistry 9, 4110-4116) was treated with colchicine to stabilize it, GTP(gamma F) was added and the 254.1 MHz 19fluorine relaxation rates measured within the first four hours. Longitudinal and transversal relaxation rates were determined in the presence of colchicine-tubulin-Mn(II), (paramagnetic complex), or the ternary complex with magnesium (diamagnetic complex). The analysis of the temperature-dependent relaxation data indicates that the metal and the exchangeable nucleotide binding sites are separated by a maximal distance of 6 at 35 degrees C, to 8.1 A at 12 degrees C.
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PMID:Nuclear relaxation rates study of GTP(gamma F)-tubulin interaction using 19F-nuclear magnetic resonance. 261 17

Binding of 4-fluorobenzenesulfonamide to human carbonic anhydrases I and II has been studied by proton, fluorine, and nitrogen-15 nuclear magnetic resonance spectroscopy. All three types of experiments provide evidence that the stoichiometry of the interaction of this inhibitor with both enzymes is 2 mol of inhibitor bound per mole of enzyme. Observations which suggest that the bound forms are involved in an exchange process that is rapid at room temperature but slower at 2 degrees C are described. Nitrogen-15 shift data show that the bound inhibitors are present at the active site as anions. The proton experiments indicate appreciable reorganization of the tertiary structure of the protein upon binding. Saturation-transfer experiments to determine the rate of dissociation of the inhibitor-enzyme complex lead to the conclusion that the dissociation process is more complicated than a simple free-bound equilibrium.
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PMID:NMR studies of carbonic anhydrase-4-fluorobenzenesulfonamide complexes. 313 26

To determine whether tubulin polymerization requires the bivalent metal-GTP complex with the gamma-phosphate in the dianionic form, the effect of GTP(gamma F) on the polymerization process was studied, in the presence of either magnesium or manganese. P3-fluoro P1-5'-guanosine triphosphate (GTP(gamma F)) was a competitive inhibitor (Ki = 1.8 X 10(-4) M) of the GTPase activity of tubulin-colchicine complex, stopped the polymerization process during the course of reaction and no depolymerization occurred. This indicates that GTP(gamma F) has access only to the nucleotide exchangeable site of the free tubulin dimer. Tubulin has one mole of magnesium tightly bound per mole of dimer. In order to know whether the inhibitory effect of GTP(gamma F) was due to the release of the metal, magnesium was replaced for manganese (a paramagnetic ion) and the paramagnetic effect of manganese on the fluorine NMR signal from the GTP(gamma F)-tubulin-metal complex was followed. Longitudinal and transversal relaxation rates measurements of the 1 degree F-NMR signal allowed to determine that the upper distance from the manganese site to the fluorine atom was between 6 and 8 A. These studies demonstrate that the dianionic form of the terminal phosphate of the metal-GTP complex, at the nucleotide exchangeable site, is essential to stimulate tubulin polymerization.
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PMID:Role of the dianionic form of the GTP gamma-phosphate in the polymerization process of tubulin. 391 58

By forward alpha scattering technique (FAST) light elements, from hydrogen through fluorine, are shown to be determined nondestructively and simultaneously, though these elements cannot be measured satisfactorily by any other physical method. We have studied on the application of this method to atmospheric aerosol, photochemical and aerosol, etc. It was assured that the whole mole ratio of aerosol can be determined by the cooperative application of the FAST and the conventional fluorescent X-ray analysis. FAST has been realized to give the water content of aerosol, although the sample should be analyzed in vacuum.
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PMID:[Analysis of aerosols for light elements by forward alpha scattering technique]. 650 95

The solution conformations of a set of uridine 2',3'-dideoxynucleosides, where each of the hydrogens at the 2'- and 3'-positions of the sugar ring were individually replaced with a fluorine atom, were studied by nuclear magnetic resonance spectroscopy and pseudorotational analysis. The distribution of the north/south (N/S) puckering equilibrium for each compound was calculated by coupling constant analysis aided by the program PSEUROT. The data confirmed that the pseudorotational equilibrium of the fluorinated glycones is governed by the position of the fluorine atom. The preferred rotamer populations about the C4'-C5' (gamma) and C1'-N1' (chi) bonds calculated from coupling constant and NOE analysis, respectively, were also influenced by the presence of fluorine. Proton coupling to the fluorine atom was also used to qualitatively estimate the N/S equilibrium population. Through space, long range 1H-19F coupling constants were observed in compounds where the fluorine atom was above the plane of the ring ('up'). The pseudorotational parameters of the compounds described were tempered by the anomeric effect which drives the pseudorotational equilibrium towards the 2'-exo/3'-endo (northern) pucker. Ab initio calculations using the 3-21 G* basis set yielded a measure of the energy differences between the N and S local minima in each compound. These results agree with previous conformational studies of other fluorinated nucleoside analogues and prove that the furanose ring pucker is governed by the highly electronegative fluorine atom. However, the competing anomeric effect plays a major role in determining the mole fraction of the minor conformer of these compounds in solution.
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PMID:Conformational analysis of the complete series of 2' and 3' monofluorinated dideoxyuridines. 908 81

Specimens of an experimental glass-ionomer cement were stored in water (initial pH 5.9) and aqueous lactic acid (initial pH 2.7) for storage periods of 1 week up to 6 weeks. Change in mass, solution pH and fluoride release were measured at weekly intervals, and other ions were determined at weeks 1, 2, 4 and 6. In water, cements raised the pH consistently to 6.7-6.9 from weeks 2 to 6, but this did not correspond to uniform amounts of ions released, nor even to consistent mole ratios of ions in solution. Similarly, in lactic acid, pH was raised to between 3.6 and 4.5, but without a consistent concentration of ions in solution. In near neutral conditions, calcium was found to be virtually insoluble and remained within the cement, whereas reasonable amounts of sodium, aluminium, phosphorus, silicon and fluoride were released at all time intervals, with downward trends over time. In acidic conditions, considerable amounts of calcium were released over time, and amounts of calcium, aluminium, phosphorus and silicon increased with time, reaching a maximum in week 4. This suggests that as maturation proceeds, there is an increase in the acid-soluble fraction of the cement containing these elements. Fluoride release was found to be as previously reported, i.e. greater amounts in the early stages of the experiment, and with a gradual decline, and with greater amounts in acid than in water. Determination of fluoride with and without the decomplexing reagent TISAB showed that 70-75% of the total fluoride was released in "free" form in water for most weeks, whereas in acid, it declined sharply and by week 6, an estimated total of 96% of the fluoride released was complexed.
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PMID:Buffering and ion-release by a glass-ionomer cement under near-neutral and acidic conditions. 1205 29

The in vitro biocompatibility of a group of ionomeric cements (ICs) was evaluated with respect to their ion release properties. These ICs were made from a defined series of glasses with the general formula 1.5SiO2.0.5P2O5.Al2O3.(1.0-Z)CaO.0.75CaF2 where Z was the mole fraction (ranging from 0-0.1) of an alkali metal oxide, either sodium or potassium or a mixture of both. For these alkali metal ICs, the amount of sodium released was directly related to the sodium content of the constituent glass. Similarly, the amount of potassium released was directly related to the potassium content. There was no correlation between the aluminum content of the glass and the aluminum ion release. Increasing the monovalent cation concentration, however, produced ICs with increased fluoride release. The biocompatibility of the ICs, as assessed by in vitro cell growth and viability measurements, was inversely proportional to aluminum ion release. Fluoride ion release, although important in terms of in vitro biocompatibility, would appear to be less important than aluminum ion release in determining the overall biocompatibility of the ICs studied.
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PMID:Dependence of in vitro biocompatibility of ionomeric cements on ion release. 1534 32


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