324 research outputs found

    Symptomatic Hypocalcemia in Primary Hyperaldosteronism: A Case Report

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    The metabolic alterations caused by hyperaldosteronism are being increasingly recognized and have generated considerable interest among the medical fraternity. Hyperaldosteronism is suspected to have a pivotal role in the patho-physiology of congestive cardiac failure where it has been studied extensively. But its effects on calcium metabolism, parathyroid metabolism and renal handling of calcium are less well described. Recent experimental models have shed light into the roles played by previously unknown mechanisms in causing these metabolic alterations. We hereby report a case of primary hyperaldosteronism due to adrenal adenoma (Conn's syndrome) who presented with a myriad of clinical features including symptomatic hypocalcemia, significant weight loss along with uncontrolled hypertension for a prolonged period before eventually detected to have primary hyperaldosteronism. Surgical removal of the causative tumor resulted in prompt disappearance of all the symptoms and signs and regain of lost weight

    Chronica de la provincia de Castilla, León y Navarra del Orden de la Santissima Trinidad, Redención de Cautivos : primera parte / escrivela... Francisco de la Vega y Toraya... de la misma religión

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    Precede al tit.: Ave MariaSign.: [calderón]-2[calderón]4, 3[calderón]6, A-4n4, 4ó5Texto a dos col.Port. con orla tip.Copia digital. Valladolid : Junta de Castilla y León. Consejería de Cultura y Turismo, 2009-201

    Correlations of structural, magnetic, and dielectric properties of undoped and doped CaCu3Ti4O12

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    The present work reports synthesis, as well as a detailed and careful characterization of structural, magnetic, and dielectric properties of differently tempered undoped and doped CaCu3Ti4O12 (CCTO) ceramics. For this purpose, neutron and x-ray powder diffraction, SQUID measurements, and dielectric spectroscopy have been performed. Mn-, Fe-, and Ni-doped CCTO ceramics were investigated in great detail to document the influence of low-level doping with 3d metals on the antiferromagnetic structure and dielectric properties. In the light of possible magnetoelectric coupling in these doped ceramics, the dielectric measurements were also carried out in external magnetic fields up to 7 T, showing a minor but significant dependence of the dielectric constant on the applied magnetic field. Undoped CCTO is well-known for its colossal dielectric constant in a broad frequency and temperature range. With the present extended characterization of doped as well as undoped CCTO, we want to address the question why doping with only 1% Mn or 0.5% Fe decreases the room-temperature dielectric constant of CCTO by a factor of ~100 with a concomitant reduction of the conductivity, whereas 0.5% Ni doping changes the dielectric properties only slightly. In addition, diffraction experiments and magnetic investigations were undertaken to check for possible correlations of the magnitude of the colossal dielectric constants with structural details or with magnetic properties like the magnetic ordering, the Curie-Weiss temperatures, or the paramagnetic moment. It is revealed, that while the magnetic ordering temperature and the effective moment of all investigated CCTO ceramics are rather similar, there is a dramatic influence of doping and tempering time on the Curie-Weiss constant.Comment: 10 pages, 11 figure

    Structural insights into the production of 3-hydroxypropionic acid by aldehyde dehydrogenase from Azospirillum brasilense

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    3-Hydroxypropionic acid (3-HP) is an important platform chemical to be converted to acrylic acid and acrylamide. Aldehyde dehydrogenase (ALDH), an enzyme that catalyzes the reaction of 3-hydroxypropionaldehyde (3-HPA) to 3-HP, determines 3-HP production rate during the conversion of glycerol to 3-HP. To elucidate molecular mechanism of 3-HP production, we determined the first crystal structure of a 3-HP producing ALDH, alpha-ketoglutarate-semialdehyde dehydrogenase from Azospirillum basilensis (AbKGSADH), in its apo-form and in complex with NAD(+). Although showing an overall structure similar to other ALDHs, the AbKGSADH enzyme had an optimal substrate binding site for accepting 3-HPA as a substrate. Molecular docking simulation of 3-HPA into the AbKGSADH structure revealed that the residues Asn159, Gln160 and Arg163 stabilize the aldehyde-and the hydroxyl-groups of 3-HPA through hydrogen bonds, and several hydrophobic residues, such as Phe156, Val286, Ile288, and Phe450, provide the optimal size and shape for 3-HPA binding. We also compared AbKGSADH with other reported 3-HP producing ALDHs for the crucial amino acid residues for enzyme catalysis and substrate binding, which provides structural implications on how these enzymes utilize 3-HPA as a substrate

    Characterisation of PduS, the pdu Metabolosome Corrin Reductase, and Evidence of Substructural Organisation within the Bacterial Microcompartment

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    PduS is a corrin reductase and is required for the reactivation of the cobalamin-dependent diol dehydratase. It is one component encoded within the large propanediol utilisation (pdu) operon, which is responsible for the catabolism of 1,2-propanediol within a self-assembled proteinaceous bacterial microcompartment. The enzyme is responsible for the reactivation of the cobalamin coenzyme required by the diol dehydratase. The gene for the cobalamin reductase from Citrobacter freundii (pduS) has been cloned to allow the protein to be overproduced recombinantly in E. coli with an N-terminal His-tag. Purified recombinant PduS is shown to be a flavoprotein with a non-covalently bound FMN that also contains two coupled [4Fe-4S] centres. It is an NADH-dependent flavin reductase that is able to mediate the one-electron reductions of cob(III)alamin to cob(II)alamin and cob(II)alamin to cob(I)alamin. The [4Fe-4S] centres are labile to oxygen and their presence affects the midpoint redox potential of flavin. Evidence is presented that PduS is able to bind cobalamin, which is inconsistent with the view that PduS is merely a flavin reductase. PduS is also shown to interact with one of the shell proteins of the metabolosome, PduT, which is also thought to contain an [Fe-S] cluster. PduS is shown to act as a corrin reductase and its interaction with a shell protein could allow for electron passage out of the bacterial microcompartment

    Morphology and Photoluminescence of HfO2Obtained by Microwave-Hydrothermal

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    In this letter, we report on the obtention of hafnium oxide (HfO2) nanostructures by the microwave-hydrothermal method. These nanostructures were analyzed by X-ray diffraction (XRD), field-emission gum scanning electron microscopy (FEG-SEM), transmission electron microscopy (TEM), energy dispersive X-ray spectrometry (EDXS), ultraviolet–visible (UV–vis) spectroscopy, and photoluminescence (PL) measurements. XRD patterns confirmed that this material crystallizes in a monoclinic structure. FEG-SEM and TEM micrographs indicated that the rice-like morphologies were formed due to an increase in the effective collisions between the nanoparticles during the MH processing. The EDXS spectrum was used to verify the chemical compositional of this oxide. UV–vis spectrum revealed that this material have an indirect optical band gap. When excited with 488 nm wavelength at room temperature, the HfO2nanostructures exhibited only one broad PL band with a maximum at around 548 nm (green emission)

    Radical SAM enzyme QueE defines a new minimal core fold and metal-dependent mechanism

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    7-carboxy-7-deazaguanine synthase (QueE) catalyzes a key S-adenosyl-L-methionine (AdoMet)- and Mg[superscript 2+]-dependent radical-mediated ring contraction step, which is common to the biosynthetic pathways of all deazapurine-containing compounds. QueE is a member of the AdoMet radical superfamily, which employs the 5′-deoxyadenosyl radical from reductive cleavage of AdoMet to initiate chemistry. To provide a mechanistic rationale for this elaborate transformation, we present the crystal structure of a QueE along with structures of pre- and post-turnover states. We find that substrate binds perpendicular to the [4Fe-4S]-bound AdoMet, exposing its C6 hydrogen atom for abstraction and generating the binding site for Mg[superscript 2+], which coordinates directly to the substrate. The Burkholderia multivorans structure reported here varies from all other previously characterized members of the AdoMet radical superfamily in that it contains a hypermodified ([β [subscript 6] over α [subscript 3]]) protein core and an expanded cluster-binding motif, CX[subscript 14]CX[subscript 2]C.United States. Dept. of Energy. Office of Biological and Environmental ResearchUnited States. Dept. of Energy. Office of Basic Energy SciencesNational Center for Research Resources (U.S.) (P41RR012408)National Institute of General Medical Sciences (U.S.) (P41GM103473)National Center for Research Resources (U.S.) (5P41RR015301-10)National Institute of General Medical Sciences (U.S.) (8 P41 GM 103403-10)United States. Dept. of Energy (Contract DE-AC02-06CH11357
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