341 research outputs found

    Corporate governance ratings as a means to reduce asymmetric information

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    Can corporate governance ratings reduce problems of asymmetric information between companies and investors? To answer this question, we set out to examine the information basis for providing such ratings by reviewing corporate governance attributes that are required or recommended in laws, accounting standards and codes, respectively. After that, we scrutinize and organize the publicly available information on the methodologies actually used by rating providers. However, important details of these methodologies are treated as confidential property, thus we approach the evaluation of corporate governance ratings as a means to reduce asymmetric information in a more general manner. We propose that the rating process may be seen as consisting of two general activities, namely a data reduction phase, and a data weighting, aggregation and classification phase. Findings based on a Danish data set suggest that rating providers by selecting relevant attributes in an intelligent way can improve the screening of companies according to governance quality. In contrast, it seems questionable that weighting, aggregation and classification of corporate governance attributes considerably improve discrimination according to governance qualityNo; keywords

    Microfabricated systems applied for DNA amplification and for flow cytometry

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    Numerical Modelling of Flow and Settling in Secondary Settling Tanks

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    Ideology and the Application of Law in SS Courts: A Case Study of Legal Practice in the Third Reich

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    This article provides an empirical study of the inner workings of an institution at the ideological heart of the Nazi state, the SS courts, and analyses how they applied SS law in cases involving unlawful sexual conduct, and how they evaluated the racial characteristics of SS men standing trial. The article demonstrates (1) that the SS courts promoted what has been referred to as an 'unlimited', radical ideology. However, the analysis will also reveal how the SS courts during the war (2) gradually climbed down from a position of ideological purity when faced with realities at the front; and (3) despite their ideological core features, in several ways operated as a legal-rational bureaucracy. Towards the end of the article, the ramifications of these findings will be discussed in light of literature concerning the role of law and ideology in the Nazi state and the Third Reich's complicated relationship with modernism.This article provides an empirical study of the inner workings of an institution at the ideological heart of the Nazi state, the SS courts, and analyses how they applied SS law in cases involving unlawful sexual conduct, and how they evaluated the racial characteristics of SS men standing trial. The article demonstrates (1) that the SS courts promoted what has been referred to as an 'unlimited', radical ideology. However, the analysis will also reveal how the SS courts during the war (2) gradually climbed down from a position of ideological purity when faced with realities at the front; and (3) despite their ideological core features, in several ways operated as a legal-rational bureaucracy. Towards the end of the article, the ramifications of these findings will be discussed in light of literature concerning the role of law and ideology in the Nazi state and the Third Reich's complicated relationship with modernism.</p

    Recombinant Production of Human Aquaporin-1 to an Exceptional High Membrane Density in <em>Saccharomyces</em> <em>cerevisiae</em>.

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    In the present paper we explored the capacity of yeast Saccharomyces cerevisiae as host for heterologous expression of human Aquaporin-1. Aquaporin-1 cDNA was expressed from a galactose inducible promoter situated on a plasmid with an adjustable copy number. Human Aquaporin-1 was C-terminally tagged with yeast enhanced GFP for quantification of functional expression, determination of sub-cellular localization, estimation of in vivo folding efficiency and establishment of a purification protocol. Aquaporin-1 was found to constitute 8.5 percent of total membrane protein content after expression at 15°C in a yeast host over-producing the Gal4p transcriptional activator and growth in amino acid supplemented minimal medium. In-gel fluorescence combined with western blotting showed that low accumulation of correctly folded recombinant Aquaporin-1 at 30°C was due to in vivo mal-folding. Reduction of the expression temperature to 15°C almost completely prevented Aquaporin-1 mal-folding. Bioimaging of live yeast cells revealed that recombinant Aquaporin-1 accumulated in the yeast plasma membrane. A detergent screen for solubilization revealed that CYMAL-5 was superior in solubilizing recombinant Aquaporin-1 and generated a monodisperse protein preparation. A single Ni-affinity chromatography step was used to obtain almost pure Aquaporin-1. Recombinant Aquaporin-1 produced in S. cerevisiae was not N-glycosylated in contrast to the protein found in human erythrocytes

    Recombinant Production of Human Aquaporin-1 to an Exceptional High Membrane Density in Saccharomyces Cerevisiae

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    In the present paper we explored the capacity of yeast Saccharomyces cerevisiae as host for heterologous expression of human Aquaporin-1. Aquaporin-1 cDNA was expressed from a galactose inducible promoter situated on a plasmid with an adjustable copy number. Human Aquaporin-1 was C-terminally tagged with yeast enhanced GFP for quantification of functional expression, determination of sub-cellular localization, estimation of in vivo folding efficiency and establishment of a purification protocol. Aquaporin-1 was found to constitute 8.5 percent of total membrane protein content after expression at 15°C in a yeast host over-producing the Gal4p transcriptional activator and growth in amino acid supplemented minimal medium. In-gel fluorescence combined with western blotting showed that low accumulation of correctly folded recombinant Aquaporin-1 at 30°C was due to in vivo mal-folding. Reduction of the expression temperature to 15°C almost completely prevented Aquaporin-1 mal-folding. Bioimaging of live yeast cells revealed that recombinant Aquaporin-1 accumulated in the yeast plasma membrane. A detergent screen for solubilization revealed that CYMAL-5 was superior in solubilizing recombinant Aquaporin-1 and generated a monodisperse protein preparation. A single Ni-affinity chromatography step was used to obtain almost pure Aquaporin-1. Recombinant Aquaporin-1 produced in S. cerevisiae was not N-glycosylated in contrast to the protein found in human erythrocytes
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