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1.
Biofizika ; 45(2): 257-9, 2000.
Artigo em Russo | MEDLINE | ID: mdl-10776537

RESUMO

The time-dependent structure formation of the fullerene derivative of p-amino benzoic acid in organic solvents was studied by scanning electron microscopy. It was shown that, during storage of solutions, the structures are destroyed.


Assuntos
Ácido 4-Aminobenzoico/química , Carbono/química , Microscopia Eletrônica , Solventes
2.
Prikl Biokhim Mikrobiol ; 29(4): 526-33, 1993.
Artigo em Russo | MEDLINE | ID: mdl-8415516

RESUMO

In the presence of food fibers, proteolysis occurs with the formation of sorption complexes. At the initial stages of hydrolysis, the adsorption of both casein and pepsin is observed, the adsorption influencing the initial rate of hydrolysis. The composition of the sorption layer changes during hydrolysis in favor of intermediates. The initial and stationary rates of hydrolysis depend on the protein/fiber ratio. The catalytic activity of the system decreases both with a little amount and with an excess of fibers. The highest rate of hydrolysis is observed at a protein/fiber ratio of 1/2.


Assuntos
Caseínas/metabolismo , Fibras na Dieta , Pepsina A/metabolismo , Hidrólise , Cinética , Microscopia Eletrônica
3.
Nahrung ; 29(7): 639-50, 1985.
Artigo em Inglês | MEDLINE | ID: mdl-4047131

RESUMO

To the study of the structure and properties of the thermotropic soybean globulin fraction (SGF) gels the stress relaxation and electron microscopy techniques has been applied. The value of slope of normalized relaxation function was used as a characteristic of relaxation properties of SGF gels. This value characterizes the velocity of the gels relaxation processes. It has been found that this characteristic is determined only by the gels' heating temperatures. Using the differential scanning microcalorimetric technique it was shown that the changes of the slope of normalized relaxation function of SGF gels are controlled only by heating temperature. The reason for this lies in the changes of the composition of the denaturation product of SGF gels. The increase is shown of the shear moduli of gels prepared at other than optimum temperatures by additional heating under optimal gelation conditions. That is a result of existence of a sol-fraction. The most significant increase of shear moduli is found for the SGF gels, sol-fraction of which is native 11S globulin. A correlation has been established between the changes of SGF gels' structure obtained from the dates of rheological measurements and electron microscopy technique.


Assuntos
Globulinas/análise , Glycine max/análise , Varredura Diferencial de Calorimetria , Fenômenos Químicos , Físico-Química , Elasticidade , Géis , Microscopia Eletrônica , Temperatura , Viscosidade
4.
Biofizika ; 28(6): 958-61, 1983.
Artigo em Russo | MEDLINE | ID: mdl-6652133

RESUMO

An attempt was made to estimate the quality of cryofixation by thermogram method--time relationship of object temperature during freezing and heating of the specimen while preparing it for the electron microscopic studies. The experiments carried out showed the necessity of estimating cryofixation quality to rule out artefacts appearing due to solvent crystallization.


Assuntos
Microscopia Eletrônica , Manejo de Espécimes/métodos , Cristalização , Congelamento
6.
Biofizika ; 25(4): 610-4, 1980.
Artigo em Russo | MEDLINE | ID: mdl-6251918

RESUMO

Air-dry collagen isolated from cattle retinal layer by means of alkaline-salt treatment was crushed in a laboratory vibro-mill at 80-150 degrees K. Mechanochemical transformations were studied by means of viscosimetry, polarimetry, ESR-spectroscopy and electron microscopy. Mechanical tensions induce breakage of covalent bonds of polypeptide chains, accompanied by a decrease of protein molecular mass, and of lateral interactions, which results in loosening of collagen structure and partial denaturation.


Assuntos
Colágeno , Fenômenos Químicos , Físico-Química , Espectroscopia de Ressonância de Spin Eletrônica , Microscopia Eletrônica , Peso Molecular , Conformação Proteica , Viscosidade
7.
Biofizika ; 25(3): 405-8, 1980.
Artigo em Russo | MEDLINE | ID: mdl-7190442

RESUMO

Comparative studies of some biological subjects with different water content (yeast cells, swollen starch grains, gels and gelatin and casein solutions) were conducted in scanning and transmitting electron electron microscope. The objects were prepared by cryogenic methods: freezing--drying; freezing--fracture, freezing--etching. It has been shown that when interpreting the micrographs of scanning microscopy for the systems biopolymer--water it is useful to apply the results of transmitting microscopy by using different procedures of preparation both with dehydration and without dehydration of the object. The electron micrographs have shown that with a rise in water content in the object the probability of artefact occurrence is increased for the objects studied in the scanning microscope by using freezing--drying method.


Assuntos
Biopolímeros , Substâncias Macromoleculares , Microscopia Eletrônica/métodos , Água , Caseínas , Liofilização/métodos , Técnica de Congelamento e Réplica/métodos , Técnica de Fratura por Congelamento/métodos , Gelatina , Globulinas , Microscopia Eletrônica de Varredura/métodos , Proteínas de Plantas , Glycine max/análise
8.
Biofizika ; 24(4): 637-9, 1979.
Artigo em Russo | MEDLINE | ID: mdl-38855

RESUMO

Electron microscopic study was carried out of the structure of pectin 0.01% aqueous solutions according to esterification degree at different pH medium. Preparations were prepared by freezing-drying method of solution drop on the formvar film and by the negative contrasting method. Microfibrils of 60-180 A diameter were found. Their aggregation increased with a decrease of the charge of pectin macromolecule (increase of esterification, decrease of pH).


Assuntos
Pectinas , Fenômenos Químicos , Química , Esterificação , Concentração de Íons de Hidrogênio , Microscopia Eletrônica , Soluções
9.
Biofizika ; 24(3): 438-41, 1979.
Artigo em Russo | MEDLINE | ID: mdl-465550

RESUMO

Comparative electron microscopic investigation of submolecular structure formation of native collagen molecules and denaturated collagen peptides in tropocollagen and gelatin gels was carried out. Submolecular terminal structures were similar. Fibrils exist with cross striation region of 64--70 nm. In spite of this the intermediate steps in the formation of both structures differ. In case of collagen the bundle of parallel microfibrils forms the thick fibrils. In case of gelatin the aggregates of spherical anisotropic particles form the fibrils of gelatin gels.


Assuntos
Colágeno , Fenômenos Químicos , Físico-Química , Gelatina , Géis , Microscopia Eletrônica , Conformação Proteica , Temperatura , Tropocolágeno
10.
Biofizika ; 24(1): 172-3, 1979.
Artigo em Russo | MEDLINE | ID: mdl-435533

RESUMO

When using low temperature methods for preparing water-containing objects in electron microscopy temperature characteristics of different objects was studied during freezing and defreezing depending on different preparation conditions. Temperature characteristics of the object was estimated by means of a storage oscillograph with a thermocouple connected through a transistor amplifier. The thermograms permit one to select preparation conditions of the object eliminating artefacts.


Assuntos
Técnica de Congelamento e Réplica , Músculos , Humanos , Pessoa de Meia-Idade , Temperatura
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