1,059 research outputs found

    Energy and nutrient dietary reference values for children in Europe: methodological approaches and current nutritional recommendations

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    The Expert Group on the Methodological Approaches and Current Nutritional Recommendations in Children and Adolescents was convened to consider the current situation across Europe with regard to dietary recommendations and reference values for children aged 2-18 years. Information was obtained for twenty-nine of the thirty-nine countries in Europe and a comprehensive compilation was made of the dietary recommendations current up to September 2002. This report presents a review of the concepts of dietary reference values and a comparison of the methodological approaches used in each country. Attention is drawn to the special considerations that are needed for establishing dietary reference values for children and adolescents. Tables are provided of the current dietary reference values for energy and for the macronutrients, vitamins, minerals, trace elements and water. Brief critiques are included to indicate the scientific foundations of the reference values for children and to offer, where possible, an explanation for the wide differences that exist between countries. This compilation demonstrated that there are considerable disparities in the perceived nutritional requirements of European children and adolescents. Although some of this diversity can be attributed to real physiological and environmental differences, most is due to differences in philosophy about the best methodological approach to use and in the way the theoretical approaches are applied. The report highlights the main methodological and technological issues that will need to be resolved before harmonisation can be fully considered. Solving these issues may help to improve the quality and consistency of dietary reference values across Europe. However, there are also considerable scientific and political barriers that will need to be overcome and the question of whether harmonisation of dietary reference values for children and adolescents is a desirable or achievable goal for Europe requires further consideratio

    Organic facies of the Frome Embayment and Callabonna Sub-basin: what and where are the uranium reductants?

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    Bernd H Michaelsen, Adrian J Fabris, John L Keeling, David M McKirdy, Laszlo F Katona and Les R Tucke

    The Solution Structures of Two Human IgG1 Antibodies Show Conformational Stability and Accommodate Their C1q and FcγR Ligands.

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    The human IgG1 antibody subclass shows distinct properties compared with the IgG2, IgG3, and IgG4 subclasses and is the most exploited subclass in therapeutic antibodies. It is the most abundant subclass, has a half-life as long as that of IgG2 and IgG4, binds the FcγR receptor, and activates complement. There is limited structural information on full-length human IgG1 because of the challenges of crystallization. To rectify this, we have studied the solution structures of two human IgG1 6a and 19a monoclonal antibodies in different buffers at different temperatures. Analytical ultracentrifugation showed that both antibodies were predominantly monomeric, with sedimentation coefficients s20,w (0) of 6.3-6.4 S. Only a minor dimer peak was observed, and the amount was not dependent on buffer conditions. Solution scattering showed that the x-ray radius of gyration Rg increased with salt concentration, whereas the neutron Rg values remained unchanged with temperature. The x-ray and neutron distance distribution curves P(r) revealed two peaks, M1 and M2, whose positions were unchanged in different buffers to indicate conformational stability. Constrained atomistic scattering modeling revealed predominantly asymmetric solution structures for both antibodies with extended hinge structures. Both structures were similar to the only known crystal structure of full-length human IgG1. The Fab conformations in both structures were suitably positioned to permit the Fc region to bind readily to its FcγR and C1q ligands without steric clashes, unlike human IgG4. Our molecular models for human IgG1 explain its immune activities, and we discuss its stability and function for therapeutic applications
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