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1.
J Nutr Health Aging ; 13(9): 782-8, 2009 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-19812868

RESUMO

OBJECTIVE: To validate a revision of the Mini Nutritional Assessment short-form (MNA(R)-SF) against the full MNA, a standard tool for nutritional evaluation. METHODS: A literature search identified studies that used the MNA for nutritional screening in geriatric patients. The contacted authors submitted original datasets that were merged into a single database. Various combinations of the questions on the current MNA-SF were tested using this database through combination analysis and ROC based derivation of classification thresholds. RESULTS: Twenty-seven datasets (n=6257 participants) were initially processed from which twelve were used in the current analysis on a sample of 2032 study participants (mean age 82.3y) with complete information on all MNA items. The original MNA-SF was a combination of six questions from the full MNA. A revised MNA-SF included calf circumference (CC) substituted for BMI performed equally well. A revised three-category scoring classification for this revised MNA-SF, using BMI and/or CC, had good sensitivity compared to the full MNA. CONCLUSION: The newly revised MNA-SF is a valid nutritional screening tool applicable to geriatric health care professionals with the option of using CC when BMI cannot be calculated. This revised MNA-SF increases the applicability of this rapid screening tool in clinical practice through the inclusion of a "malnourished" category.


Assuntos
Avaliação Geriátrica , Desnutrição/diagnóstico , Avaliação Nutricional , Inquéritos e Questionários/normas , Idoso , Idoso de 80 Anos ou mais , Antropometria , Índice de Massa Corporal , Feminino , Indicadores Básicos de Saúde , Humanos , Masculino , Desnutrição/epidemiologia , Programas de Rastreamento/métodos , Programas de Rastreamento/normas , Estado Nutricional , Curva ROC , Sensibilidade e Especificidade
2.
Comput Methods Programs Biomed ; 94(1): 88-95, 2009 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-19062126

RESUMO

The attributable risk (AR) is an epidemiologic measure quantifying the relationship between an exposure factor and a disease at the population level. In addition to its original use as a one-dimensional parameter the AR is increasingly applied in multifactorial epidemiologic situations when the combined impact of multiple exposure factors has to be partitioned into factor-specific components. We discuss the point and interval estimation of the resulting multidimensional parameter termed partial attributable risk (PAR) and introduce the R-package 'pARccs', a comprehensive software enabling the application of the methods. 'pARccs' allows for point and interval estimation of PAR from case-control data utilizing the non-parametric bootstrap with stratified resampling in combination with the percentile or BC(a) method to compute confidence intervals. We illustrate the concept of partial attributable risks and the application of the software by an example from a recent case-control study on risk factors for melanoma. We also discuss practical aspects of the software application for epidemiologic purposes and its limitations.


Assuntos
Estudos Epidemiológicos , Software , Estudos de Casos e Controles , Humanos , Medição de Risco
3.
Biotechnol Bioeng ; 69(1): 83-90, 2000 Jul 05.
Artigo em Inglês | MEDLINE | ID: mdl-10820334

RESUMO

During recombinant E. coli fermentation with high-expression levels inclusion bodies are often formed. Aqueous two-phase systems have been successfully used in the presence of urea for the initial recovery step of inclusion bodies from E. coli. Basic studies of the complex interactions are lacking. For a systematic study of protein partitioning in the presence of urea we selected T4-lysozyme mutants with different thermal stability as a model. The stabilization of these variants by phase components was investigated measuring the fluorescence emission of tryptophan residues in the protein. Protein structure was stabilized at pH 7 in the order of S0(4)(2-) >> PEG = Dextran > H(2)O. The conformation of proteins was shown to have a strong influence on the partitioning in aqueous two-phase systems. Tryptophan and its homologuous di- and tripeptdides were partitioned in similar phase systems to normalize for contribution from hydrophobic interactions.


Assuntos
Bacteriófago T4/enzimologia , Muramidase/isolamento & purificação , Ureia/química , Escherichia coli/genética , Muramidase/química , Dobramento de Proteína , Proteínas Recombinantes/química , Proteínas Recombinantes/isolamento & purificação , Triptofano/isolamento & purificação
4.
Biotechnol Prog ; 15(3): 493-9, 1999.
Artigo em Inglês | MEDLINE | ID: mdl-10356268

RESUMO

During recombinant Escherichia coli fermentation with high expression levels, inclusion bodies are often formed. Aqueous two-phase systems have been used in the presence of urea for the initial recovery steps. To investigate phase behavior of such systems we determined phase diagrams of poly(ethylene glycol) (PEG)/sodium sulfate/urea/water and PEG/dextran T-500 (DEX)/urea/phosphate buffer/water at different concentrations of urea and different molecular weight of PEG. PEG/Na2SO4 aqueous two-phase systems could be obtained including up to 30% w/w urea at 25 degrees C and PEG/dextran T-500 up to 35% w/w urea. The binodial was displaced toward higher concentrations with increasing urea concentrations. The partition coefficient of urea was near unity. An unstable mutant of T4-lysozyme with an amino acid replacement in the core (V149T) was used to analyze the effect of phase components on the conformation of the enzyme. We showed that partitioning of tryptophan was not dependent on the concentration of urea in the phase system.


Assuntos
Proteínas Recombinantes/isolamento & purificação , Substituição de Aminoácidos , Biotecnologia , Estabilidade Enzimática , Escherichia coli/genética , Escherichia coli/metabolismo , Corpos de Inclusão/metabolismo , Muramidase/química , Muramidase/genética , Muramidase/isolamento & purificação , Mutação Puntual , Conformação Proteica , Proteínas Recombinantes/química , Proteínas Recombinantes/genética , Triptofano , Ureia , Água
5.
Biophys J ; 73(6): 3211-24, 1997 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-9414232

RESUMO

The diffusion of hen egg-white lysozyme has been studied by dynamic light scattering in aqueous solutions of ammonium sulfate as a function of protein concentration to 30 g/liter. Experiments were conducted under the following conditions: pH 4-7 and ionic strength 0.05-5.0 M. Diffusivity data for ionic strengths up to 0.5 M were interpreted in the context of a two-body interaction model for monomers. From this analysis, two potential-of-mean-force parameters, the effective monomer charge, and the Hamaker constant were obtained. At higher ionic strength, the data were analyzed using a model that describes the diffusion coefficient of a polydisperse system of interacting protein aggregates in terms of an isodesmic, indefinite aggregation equilibrium constant. Data analysis incorporated multicomponent virial and hydrodynamic effects. The resulting equilibrium constants indicate that lysozyme does not aggregate significantly as ionic strength increases, even at salt concentrations near the point of salting-out precipitation.


Assuntos
Muramidase/química , Sulfato de Amônio , Animais , Fenômenos Biofísicos , Biofísica , Galinhas , Difusão , Eletrólitos , Feminino , Concentração de Íons de Hidrogênio , Técnicas In Vitro , Luz , Substâncias Macromoleculares , Modelos Químicos , Concentração Osmolar , Espalhamento de Radiação , Soluções , Água
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