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1.
Voen Med Zh ; 331(11): 20-4, 2010 Nov.
Article in Russian | MEDLINE | ID: mdl-21395155

ABSTRACT

The article is concerned with the study of use of physical factors in the treatment of chronic lymphphleboid failure of lower limbs. As a result, it was able to show a significant positive dynamic under the complex approach of treating this disease. In patients with chronic lymphphleboid failure of lower limbs justified individual tactics, based on the use of a wide range of modern medicines, physical therapy techniques, therapeutic exercises, lymphatic massage of the lower limbs. This leads to early rehabilitation and improvement of quality of patients' life.


Subject(s)
Lower Extremity/blood supply , Lymphedema/therapy , Physical Therapy Modalities , Postthrombotic Syndrome/therapy , Varicose Veins/therapy , Adult , Combined Modality Therapy , Endovascular Procedures/methods , Female , Humans , Lymphedema/diagnosis , Lymphedema/rehabilitation , Lymphedema/surgery , Male , Postthrombotic Syndrome/diagnosis , Postthrombotic Syndrome/rehabilitation , Postthrombotic Syndrome/surgery , Treatment Outcome , Varicose Veins/diagnosis , Varicose Veins/rehabilitation , Varicose Veins/surgery
2.
Anal Biochem ; 270(1): 69-74, 1999 May 15.
Article in English | MEDLINE | ID: mdl-10328766

ABSTRACT

The marine polyp Obelia longissima produces a protein, obelin, which emits light in a calcium-dependent manner. This photoprotein consists of a stable complex of its apoprotein, a chromophore, and oxygen. In the presence of calcium ions, the protein undergoes a change in conformation that allows it to catalyze the oxidation of the chromophore, coelenterazine, to coelenteramide with the release of light and CO2. Photoproteins are attractive as labels in analytical applications because the bioluminescent signal that they produce is the result of a chemical reaction and, therefore, has virtually no background. Thus, bioluminescence allows for extremely sensitive detection. In that regard, the feasibility of using obelin as a label has been explored with the development of a competitive immunoassay for the determination of a small peptide analyte. To attach the obelin label in a controlled manner to the octapeptide, a fusion protein was produced using recombinant DNA techniques. The protein consisted of the C-terminus of the peptide fused to the N-terminus of obelin. The octapeptide-obelin fusion protein retained the bioluminescence properties of the native protein, and was subsequently used to generate dose-response curves for the free octapeptide.


Subject(s)
Genetic Engineering , Luminescent Proteins/genetics , Oligopeptides/analysis , Animals , Antibodies, Monoclonal , Binding Sites , Calcium/metabolism , Carbon Dioxide/metabolism , Hydra , Light , Luminescent Measurements , Oligopeptides/genetics , Oxygen/metabolism , Recombinant Fusion Proteins/analysis
3.
Trends Cardiovasc Med ; 9(8): 221-5, 1999 Nov.
Article in English | MEDLINE | ID: mdl-11094329

ABSTRACT

Class B scavenger receptors are predominantly localized to cholesterol and sphingomyelin-enriched domains within the plasma membrane, called caveolae. Caveolae and their associated protein, caveolin, have been implicated in cholesterol trafficking and in the regulation of cellular cholesterol homeostasis. Recent studies indicate that scavenger receptor, class B, type I (SR-BI) mediates cholesterol flux between cells and lipoproteins. Caveolae appear to be the sites within the plasma membrane where such exchange occurs, suggesting that the regulation of caveolae and caveolins may be pivotal to the net flux of cholesterol between cells and lipoproteins when they are bound to SR-BI.


Subject(s)
Caveolae/metabolism , Cholesterol/metabolism , Homeostasis/physiology , Membrane Proteins , Receptors, Immunologic/metabolism , Receptors, Lipoprotein , CD36 Antigens , Caveolins/metabolism , Cell Membrane/metabolism , Humans , Receptors, Scavenger , Scavenger Receptors, Class B
4.
Biochim Biophys Acta ; 1293(2): 207-12, 1996 Apr 16.
Article in English | MEDLINE | ID: mdl-8620031

ABSTRACT

A sensitive assay which examines the effects of ATP level on the overall activity of a cell-free translation system in a protein synthesis is described. The translational activity of cell-free system was measured in terms of a rate of protein synthesis directed by the 'test' template. The test template encodes a photoluminescent protein, obelin accumulation was determined from the kinetic curves of obelin. The rate of obelin mRNA translation. Time-dependent nucleotide level measurements were conducted throughout the translation processes. It has been shown that the rate of translation decreases exponentially with the decrease of the ATP level. This fall in the overall translation rate is due in part to the mRNA becoming inactive in the translation process. This is not caused by degradation, this mRNA can be restored for translation in a fresh cell-free system by phenol treatment. The reported results provide evidence that the level of ATP unambiguously determines the translational activity of the system.


Subject(s)
Adenosine Triphosphate/metabolism , Luminescent Proteins/biosynthesis , Protein Biosynthesis , Adenosine Diphosphate/metabolism , Adenosine Monophosphate/metabolism , Adenosine Triphosphate/pharmacology , Cell-Free System/metabolism , Kinetics , Linear Models , RNA, Messenger/metabolism , Triticum
5.
Anal Biochem ; 231(1): 34-9, 1995 Oct 10.
Article in English | MEDLINE | ID: mdl-8678317

ABSTRACT

Obelin mRNA obtained in vitro with the aid of SP6 RNA polymerase was translated in a wheat germ cell-free system. Only the polypeptide with a molecular mass of about 20 kDa was synthesized. The activation of apoobelin with a synthetic coelenterazine revealed a luminescence activity initiated by calcium. The specific activity was 3.6 +/- 0.4 x 10(15)photons per mg of the in vitro synthesized obelin (k=6.9s(-1)). The luminescence of the obelin was in a good correlation with the protein concentration calculated by the incorporation of [14C]Leu. The determination of the amount of de novo synthesized obelin based on measurement of its luminescence is one-thousand times more sensitive than the approach based on the incorporation of labeled amino acid. Thus, obelin mRNA has some advantages for evaluating the efficiency of cell-free translation when compared with standard methods.


Subject(s)
Luminescent Proteins/genetics , Protein Biosynthesis , RNA, Messenger/genetics , Cell-Free System , Luminescent Proteins/metabolism , RNA, Messenger/metabolism
6.
Int J Rad Appl Instrum A ; 40(8): 711-3, 1989.
Article in English | MEDLINE | ID: mdl-2548979

ABSTRACT

The radionuclide 152Eu was produced by irradiating 151Eu2O3 or 151EuCl3 enriched to 98.9% with thermal neutrons. 152Eu was separated from rare-earth impurities by extraction chromatography on a column using 0.6 M nitric acid eluent. The specific activity of the 152Eu was 1-10 Ci/g of Eu. The impurity of the 154Eu did not exceed 0.1%. The activity standardization of 152Eu was carried out by extrapolation of 4 pi (beta, e, x)-gamma coincidences. The relative gamma-ray intensities for 28 gamma-ray energies emitted in 152Eu decay have been measured.


Subject(s)
Europium , Radioisotopes , Spectrophotometry/instrumentation , Gamma Rays , Spectrophotometry/methods
8.
Mol Biol (Mosk) ; 16(6): 1234-44, 1982.
Article in Russian | MEDLINE | ID: mdl-6759922

ABSTRACT

Melting of the 5S RNA from E. coli ribosomes has been studied by differential scanning microcalorimetry. It has been shown that: (1) heat capacity temperature functions of the "native" and A-forms of the 5S RNA coincide in all the conditions studied; (2) heat capacity temperature functions of the B-form of the 5S RNA differ in a low-temperature region from the heat capacity functions of the A-form, the complete melting enthalpy of the A-form being higher by 125 +/- 30 kJ X M-1; (3) the teritary structure of the 5S RNA does not unite secondary structure elements into a single cooperative unit even in the presence of 10 mM MgCl2; (4) the results of the analysis of the "equilibrium" part of heat capacity temperature functions and the A- and B-forms of the 5S RNA can be explained by melting of four cooperative blocks which interact with each other.


Subject(s)
Escherichia coli/ultrastructure , RNA, Ribosomal , Ribosomes/ultrastructure , Calorimetry, Differential Scanning , Molecular Weight , Thermodynamics
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