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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The purpose of this study was to physiologically characterize the basolateral Na(+)/Ca(2+) exchanger (NCX) in basolateral membrane vesicles (BLMVs) of hepatopancreas and antennal gland of intermolt crayfish. Conditions were optimized to measure Na(+)-dependent Ca(2+) uptake and retention in the BLMV including use of intravesicular (IV) oxalate and measuring initial uptake rates at 20 s. Na(+)-dependent Ca(2+) uptake rate into BLMV was temperature insensitive. Na(+)-dependent Ca(2+) uptake rate was dependent upon free Ca(2+) with saturable Michaelis-Menten kinetics determined as follows: hepatopancreas, maximal uptake rate (J(max))=2.45 nmol/mg per min, concentration at which carrier operates at half-maximal uptake rate (K(m))=0.69 microM Ca(2+); antennal gland, J(max)=13.2 nmol/mg per min, K(m)=0.59 microM Ca(2+). The two vesicle populations exhibited different sensitivity to putative NCX inhibitors. Benzamil had no effect on Na(+)-dependent Ca(2+) uptake rate in hepatopancreas; in antennal gland it was inhibitory at concentrations up to 30 microM and was stimulatory at higher concentrations. Conversely the inhibitor quinacrine was inhibitory at 10 microM in hepatopancreas and was stimulatory at 1000 microM; meanwhile it was ineffective in antennal gland BLMV. Short circuiting the BLMV had no effect on Na(+)-dependent Ca(2+) uptake rate suggesting that the process may be electroneutral. Compared with another prominent basolateral transporter in hepatopancreas the plasma membrane Ca(2+) ATPase (PMCA), the NCX has 70-fold greater J(max) (at comparable temperature) and a lower affinity. In antennal gland the NCX has 40-fold greater J(max) and a lower affinity. In hepatopancreas and antennal gland BLMV NCX appears to determine the rate of basolateral Ca(2+) efflux in intermolt.
Comp Biochem Physiol A Mol Integr Physiol 2002 Feb
PMID:Physiological characterization of the Na(+)/Ca(2+) exchanger (NCX) in hepatopancreatic and antennal gland basolateral membrane vesicles isolated from the freshwater crayfish Procambarus clarkii. 1181 24

The Raman and infrared spectra of solid K2(12)C2O4 x H2O are reported together with, for the first time, the corresponding Raman and infrared spectra of solid K2(13)C2O4 x H2O. Raman spectra of aqueous solutions of both isotopomers are also reported. In the solid state the oxalate anion is planar with D2h symmetry in this salt, whereas in aqueous solution the Raman spectra of the anion are best interpreted on the basis of D2d symmetry. The Raman spectra of solid (NH4)2(12)C2O4 x H2O and (NH4)2(13)C2O4 x H2O, in which the oxalate anion is twisted from planarity by 28 degrees about the CC bond, have also been recorded. Several reassignments have been made. The harmonic force field for the oxalate anion in the D2h, D2 and D2d geometries has been determined in part, and approximate values of key valence force constants determined. All the observed band wavenumbers and 12C/13C isotopic shifts are well reproduced by the force fields. The potential energy distribution of the totally symmetric normal modes of planar oxalate indicates that each mode consists of extensively mixed symmetry corrdinates and that the labels previously used for the bands seen here at 475 and 879 cm(-1) would better be described as v(CC) and deltaS(CO2), respectively, putting them in the same wavenumber order as v(NN) and deltaS(NO2) for the isoelectronic and isostructural molecule N2O4. The stretching force constants of N2O4 and planar C2O4(2-) are established to be in the order f(NN) < f(CC) and f(NO) > f(CO), consistent with the known relative bond lengths.
Spectrochim Acta A Mol Biomol Spectrosc 2002 Jun
PMID:Raman, infrared and force field studies of K2(12)C2O4 x H2O and K2(13)C2O4 x H2O in the solid state and in aqueous solution, and of (NH4)2(12)C2O4 x H2O and (NH4)2(13)C2O4 x H2O in the solid state. 1216 44

This study was aimed to investigate the effect ofCyclosporin A administration on renal calcium oxalate binding under hyperoxaluric condition. Cyclosporin A administration or ammonium oxalate treatment increased calcium oxalate binding, which was further increased in kidney treated with cyclosporin A and ammonium oxalate together. The increase of calcium oxalate binding was associated with lipid peroxidation as well as with a concomitant decrease in total thiol in both rat and human kdiney homogenate. Cyclosporin A administration to hyperoxaluric rats resulted with increased calcium oxalate binding protein. However there was no change with specific activity of the protein. In conclusion, Cyclosporin A administration either to normal or hyperoxaluric rats is resulted with increased concentration of calcium oxalate binding protein as well as enhanced activity due to membrane lipid peroxidation.
Mol Cell Biochem 2002 Jul
PMID:Effect of cyclosporin A treatment on renal calcium oxalate binding in experimental hyperoxaluria. 1219 Jan 7

The chemiluminescence arising from the reaction of bis(2,4,6-trichlorophenyl)oxalate (TCPO) with hydrogen peroxide in the presence of acriflavine has been studied. The relationship between the chemiluminescence intensity and concentrations of TCPO, H2O2, acriflavine and the base sodium salicylate are reported. The kinetic parameters for the peroxyoxalate-chemiluminescence (PO-CL) of acriflavine were evaluated from the computer fitting of the corresponding chemiluminescence intensity-time plots.
Spectrochim Acta A Mol Biomol Spectrosc 2003 Feb
PMID:A study of peroxyoxalate-chemiluminescence of acriflavine. 1252 21

The crystal structure of beta-alanine-oxalic acid (1:1) hemihydrate complex has been reinvestigated by X-ray diffraction method at 293 K. Formation of monoclinic crystal system belonging to C2/c space group and consisting of semi-oxalate chains, diprotonated beta-alanine dimers and water molecules bonded to both these units is confirmed. New results are obtained for distances in the carboxylic groups and hydrogen bonds. These structural observations are used for protonation degree monitoring on the carboxylic oxygen atoms. They are in accordance with our vibrational study. The 13C NMR spectra provide insights into the solid structure of this complex, character of its hydrogen bonds and the beta-alanine protonation.
Spectrochim Acta A Mol Biomol Spectrosc 2003 Mar 01
PMID:Beta-alanine-oxalic acid (1:1) hemihydrate crystal: structure, 13C NMR and vibrational properties, protonation character. 1260 16

Both rat and human kidney nuclei exhibited time and pH dependent oxalate or histone-oxalate uptake which was inhibited by anion transport inhibitor, 4,4'-dithiocyanostilbene-2,2'-disulphonic acid. Sodium chloride had no effect. Nuclear membrane had oxalate binding at pH 7.4. Extraction of nuclear membrane by Triton-high salt mixture showed maximal oxalate binding activity with nuclear pore complex while nuclear lamin had no oxalate binding. The rat and human kidney nuclear pore complex showed oxalate binding of 144 and 220 pmoles/mg protein respectively. Subsequent purification of the protein on diethyl amino ethyl-Sephadex A 50 column and Sephadex G-200 column yielded 4-fold purification. The protein revealed a molecular weight of 205 kDa on SDS-PAGE. The protein was found to be saturable at 2 microM oxalate and had a Kd of 2.98 pM and a Bmax of 197 pmoles. Antibody for 205 kD was separated from primary biliary cirrhosis serum containing auto antibody against 205 kDa using affinity column chromatography. The oxalate binding activity as well as the nuclear uptake of oxalate or histone-oxalate were inhibited by its antibody.
Mol Cell Biochem 2003 Jan
PMID:Characterisation of nuclear pore complex oxalate binding protein from human kidney. 1261 82

A unique photochemical cell design and two experiments are presented, which illustrate the usefulness of flow-through attenuated total reflectance (ATR) Fourier transform infrared (FT-IR) spectroscopy as a technique for investigating photochemical reactions at the mineral-water interface. The kinetics of the photolysis reaction of potassium oxalate (K(2)C(2)O(4)) in a ferric iron solution and oxalate adsorbed onto goethite (alpha-FeOOH) were investigated to show the capabilities of the cell. Due to complicated kinetics, the adsorption experiment demonstrates not only the types of complex problems, that may exist at the mineral-water interface, but also the ability for this novel cell design to address them.
Spectrochim Acta A Mol Biomol Spectrosc 2003 Mar 15
PMID:A novel vertical attenuated total reflectance photochemical flow-through reaction cell for Fourier transform infrared spectroscopy. 1263 27

The interactions of dihydronicotinamide adenine dinucleotide (NADH) with Al(III) in near neutral aqueous solutions were studied by means of multinuclear (31P, 27Al, 1H and 13C)-NMR and fluorescence spectra techniques. The results suggested that Al(III) interacts with NADH by occupying the binding sites of pyrophosphate oxygen atoms and locks the adenine moiety of coenzyme in an anti folded conformation Meanwhile, the weak attractive interactions ('association') may occur between Al(III) and the hydroxyl groups of ribose rings through the intramolecular hydrogen bonding. Furthermore, at biologically relevant pH and concentrations of Al(III) and NADH (pH 6.5, C(Al)=10(-6)-10(-5) M), Al(III) could increase the amount of folded forms of NADH, which will result in reducing the coenzyme NADH activity in hollow-dehydrogenases reaction systems. However, in the presence of possible competing organic acids such as citrate, oxalate and tartate, could detoxify these Al(III) toxic effect.
Spectrochim Acta A Mol Biomol Spectrosc 2003 Sep
PMID:Multi-NMR and fluorescence spectra study the effects of aluminum(III) on coenzyme NADH in aqueous solutions. 1296 52

Yttrium reacts with 5-(4'-chlorophenylazo)-6-hydroxypyrimidine-2,4-dione (I), 5-(2'-bromophenylazo)-6-hydroxypyrimidine-2,4-dione (II), 5-(2',4'-dimethylphenylazo)-6-hydroxypyrimidine-2,4-dione (III), 5-(4'-nitro-2',6'-dichlorophenylazo)-6-hydroxypyrimidine-2,4-dione (IV), 5-(2'-methyl-4'-hydroxyphenylazo)-6-hydroxypyrimidine-2,4-dione (V) to form a dark pink complexes, having an absorption maximum at 610, 577, 596, 567 and 585 nm, respectively. The complex formation was completed spontaneously in theil buffer solution and the resulting complex was stable for at least 3 h after dilution. Under the optimum conditions employed, the molar absorptivities were found to be 1.60 x 10(4), 1.29 x 10(4), 1.96 x 10(4), 1.45 x 10(4) and 1.21 x 10(4) l mol(-1) cm(-1) and the molar ratios were (1:1) and (1:2) (M:L). The linear ranges were found within 95 microg of yttrium in 25 ml solution. One of the characteristics of the complex was its high tolerance for calcium and hence a method of separation and enrichment of microamounts of yttrium by using calcium oxalate precipitate was developed and applied to measure yttrium in nickel-base alloys. Interfering species and their elimination have been studied. The precision and recovery are both satisfactory.
Spectrochim Acta A Mol Biomol Spectrosc 2003 Sep
PMID:Spectrophotometric studies and applications for the determination of yttrium in pure and in nickel base alloys. 1296 54

The synergistic activities of oxalic acid and endopolygalacturonases are thought to be essential for full virulence of Sclerotinia sclerotiorum and other oxalate-producing plant pathogens. Both oxalic acid production and endopolygalacturonase activity are regulated by ambient pH. Since many gene products with pH-sensitive activities are regulated by the PacC transcription factor in Aspergillus nidulans, we functionally characterized a pacC gene homolog, pac1, from S. sclerotiorum. Mutants with loss-of-function alleles of the pac1 locus were created by targeted gene replacement. In vitro mycelial growth of these pac1 mutants was normal at acidic pH, but growth was inhibited as culture medium pH was increased. Development and maturation of sclerotia in culture was also aberrant in these pac1 replacement mutants. Although oxalic acid production remained alkaline pH-responsive, the kinetics and magnitude of oxalate accumulation were dramatically altered. Additionally, maximal accumulation of endopolygalacturonase gene transcripts (pg1) was shifted to higher ambient pH. Virulence in loss-of-function pac1 mutants was dramatically reduced in infection assays with tomato and Arabidopsis. Based on these results, pac1 appears to be necessary for the appropriate regulation of physiological processes important for pathogenesis and development of S. sclerotiorum.
Mol Plant Microbe Interact 2003 Sep
PMID:The Sclerotinia sclerotiorum pac1 gene is required for sclerotial development and virulence. 1297 2


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