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2.
Health Phys ; 63(4): 385-92, 1992 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-1526778

RESUMO

Dietary studies and whole-body measurements were used to estimate the intake of radiocesium and the radiation dose received by different groups of people in Norway after the Chernobyl accident. Freshwater fish, milk, and reindeer meat were the major sources for radiocesium intake. Dietary advice, together with agricultural decontamination measures, resulted in a considerable reduction in the exposure level of the population. A majority (40-80%) of the specially selected groups (farmers-hunters and Sami reindeer herdsman) changed its diet significantly after the accident. Without dietary changes, specifically a reduction in the consumption of freshwater fish and reindeer meat, the Sami group would have had a 400-700% higher radiocesium intake, and the farmers-hunters' intake would have been up to 50% higher than what they actually had experienced.


Assuntos
Acidentes , Radioisótopos de Césio , Dieta , Contaminação Radioativa de Alimentos , Reatores Nucleares , Cinza Radioativa , Contagem Corporal Total , Feminino , Humanos , Masculino , Noruega , Ucrânia
3.
Chem Phys Lipids ; 57(1): 81-6, 1991.
Artigo em Inglês | MEDLINE | ID: mdl-2060066

RESUMO

The potency of lysophosphatidylcholine to perturb protein structure was investigated by differential scanning calorimetry and rheological measurements using myosin as a model protein. At physiological ionic strength (0.15 M NaCl) 5mM lysophosphatidylcholine produced a detectable reduction in the protein's enthalpy of denaturation, while concentrations less than or equal to 2 mM had no effect. At higher salt concentrations (0.6 M NaCl) lower concentrations of lysophosphatidylcholine were needed in order to reduce the enthalpy of denaturation. Also, the changes in myosin conformation, as judged from calorimetric measurements, became more extensive as the incubation temperature for myosin-lysophosphatidylcholine systems was increased from 10 degrees to 30 degrees C. Rheological techniques allowed detection of changes in the structure of filaments of myosin (in 0.15 M) upon addition of 0.2 mM lysophosphatidylcholine. The denaturing action of lysophosphatidylcholine is compared to the more familiar detergent sodium dodecyl sulphate.


Assuntos
Lisofosfatidilcolinas/farmacologia , Miosinas/química , Desnaturação Proteica , Animais , Varredura Diferencial de Calorimetria , Bovinos , Concentração de Íons de Hidrogênio , Concentração Osmolar , Reologia , Dodecilsulfato de Sódio/farmacologia , Termodinâmica
4.
Tidsskr Nor Laegeforen ; 110(3): 391-3, 1990 Jan 30.
Artigo em Norueguês | MEDLINE | ID: mdl-2309188

RESUMO

This article describes the nutritional measures introduced to protect health after the Chernobyl accident, and the associated costs. The total value of the reindeer meat, mutton, lamb and goat meat saved as a result of such measures in 1987 amounted to approx. NOK 250 million. The measures cost approx. NOK 60 million. The resulting reduction in the radiation dose level to which the population was exposed was 450 manSv. In 1988, mutton/lamb and goat meat valued at approx. NOK 310 million was saved from condemnation by similar measures, which cost approx. NOK 50 million. The resulting dose level reduction was approx. 200 manSv. The relationship (cost/benefit ratio) between the overall cost of the measures taken to reduce radioactivity levels in food and the dose level reduction achieved was acceptable.


Assuntos
Poluentes Radioativos do Ar/efeitos adversos , Poluentes Atmosféricos/efeitos adversos , Contaminação Radioativa de Alimentos/prevenção & controle , Reatores Nucleares , Proteção Radiológica/economia , Cinza Radioativa/efeitos adversos , Acidentes , Custos e Análise de Custo , Contaminação Radioativa de Alimentos/análise , Contaminação Radioativa de Alimentos/economia , Humanos , Noruega , Ucrânia
5.
Acta Chem Scand B ; 41(5): 356-61, 1987 May.
Artigo em Inglês | MEDLINE | ID: mdl-3673449

RESUMO

The absolute configuration of the more active (-)-enantiomer of the anticholinergic trihexyphenidyl hydrochloride has been established as (R) by syntheses of (S)-(+)-procyclidine hydrochloride, whose absolute configuration has been established previously, and (S)-(+)-trihexyphenidyl hydrochloride from the same chiral building block, viz. (S)-(-)-cyclohexyl-3-hydroxy-3-phenylpropanoic acid. Both enantiomers of this chiral synthon were prepared by optical resolution of the corresponding racemate, employing (R)- and (S)-1-phenylethylamine, respectively, as resolving agents.


Assuntos
Fenilpropionatos , Prociclidina/síntese química , Pirrolidinas/síntese química , Triexifenidil/síntese química , Dicroísmo Circular , Indicadores e Reagentes , Espectroscopia de Ressonância Magnética , Conformação Molecular , Rotação Ocular , Espectrofotometria Infravermelho , Estereoisomerismo
6.
Int J Pept Protein Res ; 25(6): 601-7, 1985 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-4030218

RESUMO

Conformational changes induced in ovomucoid, lysozyme and ovotransferrin on reductive addition of different sized substituents have been studied employing differential scanning calorimetry (DSC) and circular dichroic spectroscopy (CD). The thermograms obtained by DSC revealed that extensive introduction of methyl, isopropyl, cyclopentyl, cyclohexyl, benzyl or n-butyl groups has a detrimental effect on thermal stability (enthalpy of denaturation); the effect generally increases with the size of the substituent. Circular dichroic spectra were affected only to a very limited extent by the modifications, near-u.v. spectra remaining much the same while far-u.v. spectra displayed minor changes. The general conclusion drawn is that the modifications had only limited effects on the conformation of the proteins while, nonetheless, perturbing (or breaking) long-range intramolecular interactions so as to destabilize the structure. Derivatization of lysozyme and ovotransferrin with some of the larger groups has been reported to result in spontaneous precipitation of the proteins [Fretheim, K., Iwai, S. & Feeney, R.E. (1979) Int. J. Peptide Protein Res. 14, 451-456]. The present investigation indicates that precipitation was caused by (partial) denaturation (and ensuing aggregation) as a consequence of modification.


Assuntos
Conalbumina/metabolismo , Proteínas do Ovo/metabolismo , Muramidase/metabolismo , Ovomucina/metabolismo , Alquilação , Animais , Varredura Diferencial de Calorimetria , Galinhas , Dicroísmo Circular , Clara de Ovo , Feminino , Conformação Proteica , Relação Estrutura-Atividade
7.
Eur J Respir Dis ; 65(7): 512-20, 1984 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-6489486

RESUMO

The two basic proteins lysozyme and lactoferrin have been isolated from solubilized mucoid sputum from patients with chronic bronchitis in one step by cation exchange chromatography. In sputa from 13 patients with chronic bronchitis their mean concentrations were 0.4 g/l and 0.7 g/l, respectively, representing 6.6% and 11.5% of the total amount of solubilized protein. Lysozyme and the acid mucin glycoproteins of sputum formed aggregates at low ionic strength, probably as a result of electrostatic interactions between the two. Although only aggregates were formed and not a viscoelastic fluid or a gel, these interactions may contribute to the viscoelastic properties of native sputum.


Assuntos
Lactoferrina/análise , Lactoglobulinas/análise , Pneumopatias Obstrutivas/metabolismo , Muramidase/análise , Escarro/análise , Cromatografia por Troca Iônica , Humanos , Lactoferrina/metabolismo , Mucinas/metabolismo , Muramidase/metabolismo , Viscosidade
8.
Allergy ; 38(2): 131-9, 1983 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-6846739

RESUMO

Antigen 22 (ag-22) in hen's egg white, previously shown to be one of the major allergens in the egg white, was partially purified by combining biochemical separation techniques and quantitative immunoelectrophoretic methods. The molecular weight of ag-22 was found to be approximately 78,000 using analytical ultracentrifugation and pI was determined to be 6.1, which is appropriate with the values of ovotransferrin. It was concluded that ag-22 is identical with ovotransferrin. The ability of ovotransferrin to react in the human IgE-system was demonstrated in vivo and in vitro, by means of skin prick tests and crossed radioimmunoelectrophoresis.


Assuntos
Alérgenos/isolamento & purificação , Antígenos/imunologia , Proteínas do Ovo/imunologia , Clara de Ovo/efeitos adversos , Hipersensibilidade Alimentar/imunologia , Animais , Galinhas , Feminino , Hipersensibilidade Alimentar/diagnóstico , Humanos , Soros Imunes/imunologia , Soros Imunes/farmacologia , Imunoeletroforese Bidimensional , Peso Molecular , Ovalbumina/análise , Coelhos , Testes Cutâneos
10.
Eur J Respir Dis ; 61(4): 233-9, 1980 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-7202596

RESUMO

Albumin, transferrin, alpha1-acid glycoprotein, IgA, IgG, IgM, lysozyme and C3-complement factor have been immunologically determined in sputum and serum samples from 16 patients with chronic bronchitis. The sputa were effectively solubilized prior to the analysis. This is necessary for correct determination of the compositions of sputum. IgA (approx. 3 g/l) and lysozyme (approx. 1 g/l) were present in the highest concentrations. Lactoferrin was qualitatively shown to be present in all the sputa. The concentration of IgG, albumin and transferrin were much higher in the sera than in the sputa, their presence in sputum probably being a result of a passive "leakage" from serum. The ratios for IgA, IgM and lysozyme indicated that these macromolecules are locally synthesized in the respiratory tract. The concentrations of IgA and lysozyme were closely correlated, indicating that the biosynthesis of secretory IgA and bronchial lysozyme may be coupled or controlled by the same mechanism. Except for a weak correlation between the concentration of IgA in sputum and viscosity, no such correlations were obtained for the other proteins determined.


Assuntos
Pneumopatias Obstrutivas/metabolismo , Escarro/metabolismo , Complemento C3/metabolismo , Glicoproteínas/metabolismo , Humanos , Hialuronoglucosaminidase/metabolismo , Imunoglobulina A/metabolismo , Imunoglobulina G/metabolismo , Imunoglobulina M/metabolismo , Albumina Sérica/metabolismo , Transferrina/metabolismo
11.
Eur J Respir Dis ; 61(2): 84-94, 1980 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-6777179

RESUMO

Samples of sputum from nine patients with chronic obstructive lung disease were collected every morning for 5 consecutive days, and their mean apparent viscosities were determined. After a standard solubilization procedure, the concentration of immunoglobulin A (IgA) in each sample was determined by quantitative immunodiffusion and also by an immunofluorimetric method, using dimeric IgA purified from colostrum as a standard. The two methods gave diverging results probably reflecting different sensitivities of the techniques to various classes of IgA (monomers, dimers and polymers). The concentration of IgA was found to vary from 1.2 to 3.9 g/l with a mean value of 2.3 g/l for the 45 samples using the immunodiffusion technique, and from 1.3 to 4.9 g/l with a mean value of 3.5 g/l using the immunofluorimetric method. In agreement with earlier observations, a weak correlation was shown between the concentration of IgA in the samples and their mean viscosities. A similar correlation was, however, demonstrated between IgA and the total content of protein in the soluble part of the samples. It could therefore not be decided whether IgA itself or other proteins in the sputa were responsible for the observed effect on viscosity.


Assuntos
Imunoglobulina A/análise , Pneumopatias Obstrutivas/imunologia , Escarro/imunologia , Carboidratos/análise , Colostro/imunologia , Imunofluorescência , Humanos , Imunodifusão , Pneumopatias Obstrutivas/patologia , Proteínas/análise , Escarro/análise , Viscosidade
12.
Eur J Respir Dis ; 61(2): 71-6, 1980 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-7439275

RESUMO

Sputum from patients with chronic obstructive bronchitis has been fractionated on Sepharose columns after treatment with urea 6 mol/l at pH 12.5 followed by neutralization. The "mucin" fraction, which contained 70% carbohydrate and 30% protein was studied in the electron microscope after staining with phosphotungstic acid. Positively stained, thread-like, irregular contours of the mucin molecules could be demonstrated with lengths varying from 2,000 to 5,000 nm, corresponding to molecular weights between 2 X 10(6) and 6 X 10(6). This correlates fairly well with estimates from the literature of the size of these molecules.


Assuntos
Bronquite/metabolismo , Mucinas/análise , Escarro/análise , Carboidratos/análise , Fracionamento Químico , Doença Crônica , Humanos , Microscopia Eletrônica , Peso Molecular , Mucinas/isolamento & purificação , Proteínas/análise
13.
Scand J Clin Lab Invest ; 40(8): 727-31, 1980.
Artigo em Inglês | MEDLINE | ID: mdl-7280551

RESUMO

Addition of lysozyme (1 g/l) to sputum from patients with chronic obstructive lung disease increased the viscosity of the material significantly. The effect was prevented by addition of salt (LiCl) in the high concentration (0.25 mol/l). The sole addition of salt decreased the viscosity of native sputum. These results together with our earlier [5] studies of the interaction between the positively charged lysozyme and the negatively charged mucin molecules in model systems, indicate that lysozyme acts as a cross-linking agent in mucus by an electrostatic mechanism. Lysozyme is thus, at least partly, responsible for building up a macromolecular network giving mucus its characteristic gel-like properties.


Assuntos
Pneumopatias Obstrutivas/fisiopatologia , Muramidase/fisiologia , Escarro/enzimologia , Cloretos/farmacologia , Humanos , Lítio/farmacologia , Muco/enzimologia , Escarro/efeitos dos fármacos , Viscosidade
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