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1.
J Chromatogr A ; 1371: 15-19, 2014 12 05.
Artigo em Inglês | MEDLINE | ID: mdl-25458524

RESUMO

In this study multiple headspace extraction was used for the first time to measure the saturation concentration of carbon monoxide and oxygen in various ionic liquids (ILs). Many processes in ILs involve the reaction of gases so that the reactant solubility is not a mere characteristical parameter, but understanding the solubility of gases in ILs is required for assessing the feasibility of possible applications. Multiple headspace extraction has proofed to be a powerful tool to obtain solubilities in good accordance with literature data. The measured saturation concentration for carbon monoxide and oxygen in ILs based on rarely researched tetracyanoborates and other anions was in the range of 1.5-6.5mmol/L. The great advantage of multiple headspace extraction is that it is a nonexpensive method that can be realised in most analytical laboratories by combination of a simple gas chromatograph and an eligible headspace injector.

2.
Talanta ; 116: 474-81, 2013 Nov 15.
Artigo em Inglês | MEDLINE | ID: mdl-24148432

RESUMO

This paper presents a novel electrochemical membrane sensor on basis of ionic liquids for trace analysis of oxygen in gaseous atmospheres. The faradaic response currents for the reduction of oxygen which were obtained by multiple-potential-step-chronoamperometry could be used for real time detection of oxygen down to concentrations of 30 ppm. The theoretical limit of detection was 5 ppm. The simple, non-expensive sensors varied in electrolyte composition and demonstrated a high sensitivity, a rapid response time and an excellent reproducibility at room temperature. Some of them were continuously used for at least one week and first results promise good long term stability. Voltammetric, impedance and oxygen detection studies at temperatures up to 200 °C (in the presence and absence of humidity and CO2) revealed also the limitations of certain ionic liquids for some electrochemical high temperature applications. Application areas of the developed sensors are control and analysis processes of non oxidative and oxygen free atmospheres.


Assuntos
Técnicas Eletroquímicas/instrumentação , Imidazóis/química , Líquidos Iônicos/química , Oxigênio/análise , Técnicas Eletroquímicas/métodos , Eletrodos , Eletrólitos/química , Limite de Detecção , Temperatura
3.
Infect Immun ; 69(1): 472-8, 2001 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-11119539

RESUMO

Actinobacillus pleuropneumoniae, a porcine respiratory tract pathogen, has been shown to express transferrin-binding proteins and urease during infection. Both activities have been associated with virulence; however, their functional role for infection has not yet been elucidated. We used two isogenic A. pleuropneumoniae single mutants (DeltaexbB and DeltaureC) and a newly constructed A. pleuropneumoniae double (DeltaureC DeltaexbB) mutant in aerosol infection experiments. Neither the A. pleuropneumoniae DeltaexbB mutant nor the double DeltaureC DeltaexbB mutant was able to colonize sufficiently long to initiate a detectable humoral immune response. These results imply that the ability to utilize transferrin-bound iron is required for multiplication and persistence of A. pleuropneumoniae in the porcine respiratory tract. The A. pleuropneumoniae DeltaureC mutant and the parent strain both caused infections that were indistinguishable from one another in the acute phase of disease; however, 3 weeks postinfection the A. pleuropneumoniae DeltaureC mutant, in contrast to the parent strain, could not be isolated from healthy lung tissue. In addition, the local immune response-as assessed by fluorescence-activated cell sorter and enzyme-linked immunosorbent spot analyses-revealed a significantly higher number of A. pleuropneumoniae-specific B cells in the bronchoalveolar lavage fluid (BALF) of pigs infected with the A. pleuropneumoniae DeltaureC mutant than in the BALF of those infected with the parent strain. These results imply that A. pleuropneumoniae urease activity may cause sufficient impairment of the local immune response to slightly improve the persistence of the urease-positive A. pleuropneumoniae parent strain.


Assuntos
Actinobacillus pleuropneumoniae/patogenicidade , Ferro/metabolismo , Urease/fisiologia , Actinobacillus pleuropneumoniae/imunologia , Actinobacillus pleuropneumoniae/metabolismo , Animais , Anticorpos Antibacterianos/análise , Transporte Biológico , Líquido da Lavagem Broncoalveolar , Mutação , Suínos , Virulência
4.
Infect Immun ; 68(3): 1164-70, 2000 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-10678921

RESUMO

Upon iron restriction, Actinobacillus pleuropneumoniae has been shown to express the transferrin-binding proteins TbpB and TbpA, both of which have been implied to be important virulence factors. In order to identify additional iron-regulated proteins, we cloned and analyzed the region upstream of the transferrin-binding protein genes in an A. pleuropneumoniae serotype 7 strain. We located immediately upstream of the tbpB gene two open reading frames which were 43% homologous to the neisserial ExbBD protein genes. By raising specific antibodies, we showed that ExbB is expressed under iron-limiting growth conditions only, and RT-PCR analysis revealed that the exbBD genes and the tbpB gene are transcribed on a single polycistronic mRNA. By constructing an isogenic and nonpolar exbBD mutant, we showed that the exbBD genes are required by A. pleuropneumoniae for utilization of transferrin-bound iron. Using PCR and Western blotting, we showed that the genetic organization found in A. pleuropneumoniae serotype 7 is similar in all 12 A. pleuropneumoniae serotype reference strains.


Assuntos
Actinobacillus pleuropneumoniae/genética , Proteínas de Bactérias/genética , Proteínas de Transporte/genética , Proteínas de Escherichia coli , Genes Bacterianos , Ferro/metabolismo , Transferrina/metabolismo , Actinobacillus pleuropneumoniae/metabolismo , Sequência de Aminoácidos , Clonagem Molecular , Proteínas de Ligação ao Ferro , Dados de Sequência Molecular , Fases de Leitura Aberta , Transcrição Gênica , Proteínas de Ligação a Transferrina
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