386 research outputs found

    Labor Union Bankruptcy

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    Electron-Induced Dissociation of Glycosaminoglycan Tetrasaccharides

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    Electron detachment dissociation (EDD) Fourier transform mass spectrometry has recently been shown to be a powerful tool for examining the structural features of sulfated glycosaminoglycans (GAGs). The characteristics of GAG fragmentation by EDD include abundant cross-ring fragmentation primarily on hexuronic acid residues, cleavage of all glycosidic bonds, and the formation of even- and odd-electron product ions. GAG dissociation by EDD has been proposed to occur through the formation of an excited species that can undergo direct decomposition or ejects an electron and then undergoes dissociation. In this work, we perform electron-induced dissociation (EID) on singly charged GAGs to identify products that form via direct decomposition by eliminating the pathway of electron detachment. EID of GAG tetrasaccharides produces cleavage of all glycosidic bonds and abundant cross-ring fragmentation primarily on hexuronic acid residues, producing fragmentation similar to EDD of the same molecules, but distinctly different from the products of infrared multiphoton dissociation or collisionally activated decomposition. These results suggest that observed abundant fragmentation of hexuronic acid residues occurs as a result of their increased lability when they undergo electronic excitation. EID fragmentation of GAG tetrasaccharides results in both even- and odd-electron products. EID of heparan sulfate tetrasaccharide epimers produces identical fragmentation, in contrast to EDD, in which the epimers can be distinguished by their fragment ions. These data suggest that for EDD, electron detachment plays a significant role in distinguishing glucuronic acid from iduronic acid

    GC-MS Analysis of Ethanolic Extract of Pteridium Aquilinum (L.) Kuhn: An Important Fern

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    The aim of the study was to investigate the phytochemical compounds of ethanol extract of Pteridium aquilinum (L.) Kuhn using GC-MS analysis. In GC-MS analysis, 19 bioactive phytochemical compounds were identified in the ethanolic extract of Pteridium aquilinum (L.) Kuhn the components were identified by using Perkin-Elmer Gas Chromatography–Mass Spectrometry, the results of GCMS compounds in the extract was relevant to the National Institute of Standards and Technology (NIST) library. The major constituents were decane (12.1%), 1,3,7-Octatriene, 3,7-dimethyl (26.42%) and Limonene (10.89%). Keywords: Bioactive compounds, Pteridophytes, GC-MS, Pteridium aquilinum, NIS

    Structural Analysis of Heparin-Derived 3- O -Sulfated Tetrasaccharides: Antithrombin Binding Site Variants

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    Heparin is a polysaccharide that is widely used as an anticoagulant drug. The mechanism for heparin’s anticoagulant activity is primarily through its interaction with a serine protease inhibitor, antithrombin III (AT), that enhances its ability to inactivate blood coagulation serine proteases, including thrombin (factor IIa) and factor Xa. The AT-binding site in the heparin is one of the most well-studied carbohydrate-protein binding sites and its structure is the basis for the synthesis of the heparin pentasaccharide drug, fondaparinux. Despite our understanding of the structural requirements for the heparin pentasaccharide AT-binding site, there is a lack of data on the natural variability of these binding sites in heparins extracted from animal tissues. The present work provides a detailed study on the structural variants of the tetrasaccharide fragments of this binding site afforded following treatment of a heparin with heparin lyase II. The 5 most commonly observed tetrasaccharide fragments of the AT-binding site are fully characterized, and a method for their quantification in heparin and low-molecular-weight heparin products is described

    Structurally Informative Tandem Mass Spectrometry of Highly Sulfated Natural and Chemoenzymatically Synthesized Heparin and Heparan Sulfate Glycosaminoglycans

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    The highly sulfated glycosaminoglycan oligosaccharides derived from heparin and heparan sulfate have been a highly intractable class of molecules to analyze by tandem mass spectrometry. Under the many methods of ion activation, this class of molecules generally exhibits SO3 loss as the most significant fragmentation pathway, interfering with the assignment of the location of sulfo groups in glycosaminoglycan chains. We report here a method that stabilizes sulfo groups and facilitates the complete structural analysis of densely sulfated (two or more sulfo groups per disaccharide repeat unit) heparin and heparan sulfate oligomers. This is achieved by complete removal of all ionizable protons, either by charging during electrospray ionization or by Na+/H+ exchange. The addition of millimolar levels of NaOH to the sample solution facilitates the production of precursor ions that meet this criterion. This approach is found to work for a variety of heparin sulfate oligosaccharides derived from natural sources or produced by chemoenzymatic synthesis, with up to 12 saccharide subunits and up to 11 sulfo groups

    Nonlinear Parabolic Equations arising in Mathematical Finance

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    This survey paper is focused on qualitative and numerical analyses of fully nonlinear partial differential equations of parabolic type arising in financial mathematics. The main purpose is to review various non-linear extensions of the classical Black-Scholes theory for pricing financial instruments, as well as models of stochastic dynamic portfolio optimization leading to the Hamilton-Jacobi-Bellman (HJB) equation. After suitable transformations, both problems can be represented by solutions to nonlinear parabolic equations. Qualitative analysis will be focused on issues concerning the existence and uniqueness of solutions. In the numerical part we discuss a stable finite-volume and finite difference schemes for solving fully nonlinear parabolic equations.Comment: arXiv admin note: substantial text overlap with arXiv:1603.0387

    Investigating changes in the gas-phase conformation of Antithrombin III upon binding of Arixtra using traveling wave ion mobility spectrometry (TWIMS)

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    We validate the utility of ion mobility to measure protein conformational changes induced by the binding of glycosaminoglycan ligands

    Efficiency of Collisionally-activated dissociation and 193-nm photodissociation of peptide ions in fourier transform mass spectrometry

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    AbstractFor tandem mass spectrometry, the Fourier transform instrument exhibits advantages for the use of collisionally-activated dissociation (CAD). The CAD energy deposited in larger ions can be greatly increased by extending the collision time to as much as 120 s, and the efficiency of trapping and measuring CAD product ions in many times greater than the found for triple-quadrupole or magnetic sector instruments, although the increased pressure from the collision gas is an offsetting disadvantage. A novel system that uses the same laser for photodesorption of ions and their subsequent photodissociation can produce complete dissociation of larger oligopeptide ions and unusually abundant fragment ions. In comparison to CAD, much more internal energy can be deposited in the primary ions using 193-nm photons, sufficient to dissociate peptide ions of m/z > 2000. Mass spectra closely resembling ion photodissociation spectra can also be obtained by neutral photodissociation (193-nm laser irradiation of the sample) followed by ion photodesorption
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