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1.
Urologiia ; (6): 55, 57-60, 2007.
Artigo em Russo | MEDLINE | ID: mdl-18649662

RESUMO

An active substance of the drug vitaprost is a complex of water-soluble biologically active peptides isolated from bovine prostatic gland. The prostatic extract has an organ-tropic action in relation to the prostate: inhibits proliferative activity of the cells leading to suppression of prostatic adenoma development, reduces edema and activity of inflammation in prostatic diseases. The new vitaprost tablets can decrease volume of the prostate (this trend was not significant), relieve infravesical obstruction and irritation, improve quality of life. This is confirmed also by IPSS. Vitaprost tablets coated with intestinally soluble cover are recommended as a component of combined treatment of prostatic adenoma in patients with moderate infravesical obstruction irrespective of the patients' age and concomitant diseases.


Assuntos
Peptídeos/administração & dosagem , Hiperplasia Prostática/tratamento farmacológico , Adulto , Idoso , Idoso de 80 Anos ou mais , Edema/tratamento farmacológico , Humanos , Inflamação/tratamento farmacológico , Masculino , Pessoa de Meia-Idade , Peptídeos/efeitos adversos , Comprimidos com Revestimento Entérico/administração & dosagem , Comprimidos com Revestimento Entérico/efeitos adversos
2.
Bioorg Khim ; 32(5): 530-7, 2006.
Artigo em Russo | MEDLINE | ID: mdl-17042271

RESUMO

The venom of South American ant Paraponera clavata and its low-molecular-mass fraction were shown to possess insectotoxic and pore-forming activities. A number of glycophospholipid components were isolated from this ant venom by means of gel filtration and reversed-phase chromatography. Some of the compounds cause conductivity fluctuations in lipid bilayer membranes within the ranges 3-25 pS and 200-400 pS at concentrations of 10(-6) to 10(-7) M. N-Acetylglucosamine, a fatty acid, and phosphoric acid residues were found in their structures. A full structure, 3-myristoyl-2-acetamido-2-deoxy-alpha-D-glucopyranosyl phosphate, was elucidated for one of the compounds by the use of 1H, 13C, and 31P NMR spectroscopy and mass spectrometry.


Assuntos
Venenos de Formiga/análise , Glucofosfatos/química , Glicolipídeos/química , Fosfolipídeos/química , Animais , Formigas/efeitos dos fármacos , Cromatografia em Gel , Cromatografia Líquida de Alta Pressão , Espectroscopia de Ressonância Magnética , Estrutura Molecular , Fosfolipídeos/isolamento & purificação , Fosfolipídeos/toxicidade
3.
Genetika ; 40(9): 1209-14, 2004 Sep.
Artigo em Russo | MEDLINE | ID: mdl-15559148

RESUMO

The effect of heterosis was studied in several quantitative traits of clone breed and interbreed silkworm hybrids exposed to electromagnetic irradiation (lambda = 1.6 cm, power density 700 microW/cm2) during postdiapause embryonic development. The influence of the type of reproduction on the manifestation of irradiation effects in the next generation was also examined. In hybrids, the resistance to low-intensity high-frequency irradiation was higher than in the parental forms. Unlike the latter, the hybrids showed no significant modification of the traits after the exposure to electromagnetic irradiation. In the second generation, the modifying effect of irradiation is retained in the case of parthenogenetic silkworm development but not after mating.


Assuntos
Bombyx/efeitos da radiação , Vigor Híbrido/efeitos da radiação , Hibridização Genética , Característica Quantitativa Herdável , Animais , Bombyx/genética , Bombyx/fisiologia , Campos Eletromagnéticos , Desenvolvimento Embrionário/genética , Desenvolvimento Embrionário/fisiologia , Desenvolvimento Embrionário/efeitos da radiação , Vigor Híbrido/genética , Endogamia , Larva , Partenogênese/genética , Partenogênese/fisiologia , Partenogênese/efeitos da radiação , Reprodução/genética , Reprodução/fisiologia , Reprodução/efeitos da radiação
5.
Urol Nefrol (Mosk) ; (6): 45-8, 1996.
Artigo em Russo | MEDLINE | ID: mdl-9036612

RESUMO

In cases of missed preoperative diagnosis of prostatic cancer and benign hyperplasia, the recovery of unassisted urination in patients who previously have undergone transvesicular adenomectomy is often accompanied by traumatic removal of the tissues. This leads to severe anatomical changes of the cervicourethral segment in the form of postoperative strictures with occasional complete obliteration of the posterior urethra. If endoscopic correction of the posterior urethra fails to produce a persistent therapeutic effect, it is valid to perform urethral invagination into the bladder cervix according to Solovov for restoration of the bladder reservoir function, prevention of its fusion and progression of chronic interstitial cystitis. The case demonstrates successful recovery of the patency of the vesicourethral segment and capacity of the bladder in complete obliteration of the posterior urethra and small urinary bladder.


Assuntos
Adenocarcinoma/cirurgia , Complicações Pós-Operatórias/cirurgia , Neoplasias da Próstata/cirurgia , Uretra/cirurgia , Estreitamento Uretral/cirurgia , Bexiga Urinária/cirurgia , Adenocarcinoma/diagnóstico por imagem , Humanos , Masculino , Pessoa de Meia-Idade , Complicações Pós-Operatórias/diagnóstico por imagem , Prostatectomia , Neoplasias da Próstata/diagnóstico por imagem , Radiografia , Reoperação/métodos , Uretra/diagnóstico por imagem , Estreitamento Uretral/diagnóstico por imagem , Bexiga Urinária/diagnóstico por imagem
6.
J Pept Sci ; 2(3): 141-56, 1996.
Artigo em Inglês | MEDLINE | ID: mdl-9231323

RESUMO

The relation between the various spatial structures of the gramicidin A channels and their ionic conductance has been studied. For this aim, various conformations of the peptide were pre-formed in liposomal bilayer and after subsequent fusion of liposomes with planar lipid bilayer the measured channel conductance was correlated with gramicidin structures established in liposomes. To form the single-stranded pi 6.3 pi 6.3 helix the peptide and lipid were co-dissolved in TFE prior to liposome preparation. THF and other solvents were used to form parallel and antiparallel double helices. Conformation of gramicidin in liposomes made by various phosphatidylcholines was monitored by CD spectroscopy, and computer analysis of the spectra obtained was performed. After fusion of gramicidin containing liposomes with planar bilayer membranes from asolectin, the histograms of single-channel conductance were obtained. The histograms had one or three distinct peaks depending on the liposome preparation. Assignment of the structure of the channel to conductance levels was made by correlation of CD data with conductance histograms. The channel-forming analogue, des(Trp-Leu)2-gramicidin A, has been studied by the same protocol. The channel conductances of gramicidin A and the shortened analogue increase in the following order: antiparallel < parallel < pi 6.3 pi 6.3. Single-channels formed by double helices have higher dispersity of conductance than the pi 6.3 pi 6.3 helical channel. Lifetimes of the double helical and the pi 6.3 pi 6.3 helical channels are very close to each other. The data obtained were compared with theoretically predicted properties of double helices [1].


Assuntos
Gramicidina/química , Canais Iônicos/química , Sequência de Aminoácidos , Dicroísmo Circular , Condutividade Elétrica , Lipossomos/química , Lipídeos de Membrana/química , Modelos Moleculares , Dados de Sequência Molecular , Fosfatidilcolinas/química , Fosfolipídeos/química , Estrutura Secundária de Proteína , Glycine max/química , Espectroscopia de Infravermelho com Transformada de Fourier , Esfingomielinas/química
7.
Bioorg Khim ; 20(8-9): 857-71, 1994.
Artigo em Russo | MEDLINE | ID: mdl-7826413

RESUMO

A toxic principle of the Ectatomma tuberculatum ant venom called ectatomin was isolated. Ectatomin is a protein with molecular weight 7928 Da. Its complete amino acid sequence and spatial structure in aqueous solution were determined by protein chemistry methods and NMR spectroscopy techniques. Ectatomin contains two highly homologous polypeptide chains linked to each other by a disulfide bond. The chains consist of 37 and 34 amino acid residues with an internal disulfide bridge in each. In aqueous solution the molecule forms a bundle of four amphipathic alpha-helices. This toxin in a concentration of 0.05-0.01 mM forms potential dependent nonselective cation channels both in cell and artificial membranes. The channel is dimeric and the mechanism of its formation can be explained in terms of the spatial structure established.


Assuntos
Venenos de Formiga/química , Sequência de Aminoácidos , Dissulfetos/química , Espectroscopia de Ressonância Magnética , Dados de Sequência Molecular , Conformação Proteica , Relação Estrutura-Atividade
8.
FEBS Lett ; 347(2-3): 112-6, 1994 Jun 27.
Artigo em Inglês | MEDLINE | ID: mdl-8033986

RESUMO

Ectatomin (Ea) is a newly isolated main toxic component of Ectatomma tuberculatum ant venom. Structural and electrophysiological studies were performed with purified Ea. The protein consists of two homologous polypeptide chains (37 and 34 residues) and forms a four alpha-helix bundle in aqueous solution. On insertion into artificial bilayer membranes, two Ea molecules form an ion pore. Our results suggest that the 'inside-out' mechanism of pore formation requires a significant movement of Ea helical parts. The pore formation in the cell membrane might well explain the toxic activity of Ea, not excluding at the same time its intracellular activities.


Assuntos
Venenos de Formiga/química , Sequência de Aminoácidos , Animais , Venenos de Formiga/farmacologia , Venenos de Formiga/toxicidade , Membrana Celular/efeitos dos fármacos , Membrana Celular/ultraestrutura , Fenômenos Químicos , Físico-Química , Cromatografia em Gel , Cromatografia Líquida de Alta Pressão , Baratas/efeitos dos fármacos , Eletrofisiologia , Espectroscopia de Ressonância Magnética , Masculino , Camundongos , Dados de Sequência Molecular , Peso Molecular , Conformação Proteica , Estrutura Secundária de Proteína , Homologia de Sequência
9.
Khirurgiia (Mosk) ; (8): 74-5, 1993 Aug.
Artigo em Russo | MEDLINE | ID: mdl-8264176

RESUMO

The authors report on the use of an attachment for automatic regulation of vacuum intensity on a surgical electric sucking pump applied in the treatment of pneumothorax, pyopneumothorax, and pyothorax in children. The suggested attachment causes periodic removal of the exudate and air from the pleural cavity by automatic switching on of the pump and creates favorable conditions for cleansing of the cavity. The attachment of the electric sucking pump is cheap, easy in exploitation, simple in assemblage, and may be used for cleaning the pleural cavity with high precision of the necessary degree of exhaustion.


Assuntos
Pneumotórax/cirurgia , Sucção/instrumentação , Criança , Eletricidade , Desenho de Equipamento , Humanos , Supuração , Vácuo
10.
Biopolymers ; 31(4): 425-34, 1991 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-1713797

RESUMO

The conductance of the gramicidin A single channels in glycerolmonooleate membranes is strongly reduced in the presence of Mn2+ cations. The nmr experiments were performed for N-terminal to N-terminal gramicidin A dimer formed by two right-handed single-stranded helixes incorporated into the sodium dodecyl sulfate micelles in the presence of Mn2+ ions. Dependence of the nonselective spin-lattice relaxation rates of the gramicidin A protons on Mn2+ concentration was analyzed to determine coordinates of the divalent cation binding sites. It is inferred that Mn2+ ions are bound at the channel mouths at distances of 6.4, 8.6, and 8.8 A (+/- 2 A) from the oxygen atoms of exposed carbonyl groups of D-Leu 12, 14, and 10, respectively. The bounded Mn2+ retains its hydrate shell, the size of which (approximately 6 A) exceeds the inner pore diameter (approximately 4 A). That makes the gramicidin A channel impermeable for divalent cations.


Assuntos
Gramicidina/metabolismo , Canais Iônicos/metabolismo , Manganês/metabolismo , Sítios de Ligação , Cátions , Eletroquímica , Gramicidina/química , Canais Iônicos/química , Espectroscopia de Ressonância Magnética , Membranas/metabolismo , Modelos Moleculares
11.
Vopr Virusol ; 33(3): 278-81, 1988.
Artigo em Russo | MEDLINE | ID: mdl-3176426

RESUMO

The antiviral preparation 1-morpholinomethyltetrahydro-2(1H)-pyrimidinone (abbreviation DD-13) inhibiting reproduction of certain enveloped viruses belonging to groups of orthomyxoviruses and alphaviruses, influenza type A viruses among them, inhibited adsorption and insertion of influenza virus M protein into model bilayer lipid membranes. The preparation did not interact directly with lipid bilayers but, after pretreatment of M protein with it, inhibited M protein interaction with the membranes: adsorption and insertion into the bilayer DD-13 did not affect the interaction of influenza virus surface glycoproteins with the model lipid membranes. It is concluded that the DD-13 preparation, not interacting with the membranes directly, in native systems may modify the protein-lipid interactions at the stages of virus penetration into the cell, penetration of M protein-coated nucleocapsid into the cell nucleus through the nuclear membrane, as well as at the stage of virus particle assembly on the plasma membrane of the infected cell.


Assuntos
Antivirais/farmacologia , Vírus da Influenza A , Bicamadas Lipídicas/farmacologia , Pirimidinonas/farmacologia , Proteínas da Matriz Viral/farmacologia , Adsorção , Interações Medicamentosas , Técnicas In Vitro , Propriedades de Superfície
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