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1.
Klin Lab Diagn ; (3): 30-3, 2013 Mar.
Artigo em Russo | MEDLINE | ID: mdl-23808023

RESUMO

The comparative evaluation of effectiveness of different nontreponema tests in analysis of cerebrospinal fluid. The liquor from 100 patients with syphilis was analyzed using Bordet-Gengou test, VDRL test and micro-precipitation reaction with cardiolipin antigen. The Bordet-Gengou test and VDRL test made in Russia or abroad are equally effective in analysis of positive samples of liquor and twice surpass the same capacity of micro-precipitation reaction with cardiolipin antigen in case of neurosyphilis with symptoms and thrice surpass in case of asymptomatic neurosyphilis. VDRL test is a simple standardized nontreponema reaction which can substitute labor-consuming non-unified liquorologic complex in laboratory diagnostic of neurosyphilis. The testing of liquor on the basis of micro-precipitation reaction with cardiolipin antigen is non-effective and results in false negative results in Bordet-Gengou and VDRL positive tests determining high risk of erroneous clinical considerations.


Assuntos
Neurossífilis/diagnóstico , Sorodiagnóstico da Sífilis/métodos , Adulto , Idoso , Anticorpos Antibacterianos/imunologia , Cardiolipinas/imunologia , Técnicas de Laboratório Clínico , Feminino , Humanos , Masculino , Pessoa de Meia-Idade , Neurossífilis/líquido cefalorraquidiano , Neurossífilis/epidemiologia , Federação Russa , Treponema pallidum/imunologia , Treponema pallidum/isolamento & purificação , Adulto Jovem
2.
Mol Gen Mikrobiol Virusol ; (8): 16-20, 1991 Aug.
Artigo em Russo | MEDLINE | ID: mdl-1784300

RESUMO

The electrophoretic study of Yersinia pestis proteins made possible to find the significant modification of Yersinia pestis polypeptide specters when the bacteria were cultivated in semi-penetrable cells implanted into the guinea pigs peritoneum. The proteinogramms of the isolates from the implanted cells lacked the stained bands characteristic of Yersinia pestis cells grown in vitro and contained the new polypeptides absent from the bacteria grown on the Hottinger agar plates. The difference was found at the late stage of bacteria incubation in implanted cells and had the predominantly reversible characteristics. The protein of Yersinia pestis being changed in vivo is proposed to be the species specific fraction I.


Assuntos
Yersinia pestis/genética , Animais , Proteínas de Bactérias/genética , Eletroforese em Gel de Poliacrilamida , Expressão Gênica , Genes Bacterianos , Cobaias , Yersinia pestis/crescimento & desenvolvimento
4.
Biull Eksp Biol Med ; 100(10): 442-4, 1985 Oct.
Artigo em Russo | MEDLINE | ID: mdl-2996653

RESUMO

The experiments on white rats have shown that gutimin is capable of reactivating Na, K-ATPase of the synaptosomes of the jugular spinal cord in type C botulinic intoxication. Serotonin prevented Na, K-ATPase activity inhibition only in preclinical period of intoxication. Parmidin injection did not prevent suppression of Na, K-ATPase activity either in preclinical period or in skeletal muscle paresis.


Assuntos
Botulismo/tratamento farmacológico , Carbamatos/uso terapêutico , Guaniltioureia/uso terapêutico , Piridinolcarbamato/uso terapêutico , Serotonina/uso terapêutico , ATPase Trocadora de Sódio-Potássio/metabolismo , Medula Espinal/enzimologia , Tioureia/análogos & derivados , Animais , Botulismo/enzimologia , ATPase de Ca(2+) e Mg(2+)/metabolismo , Ratos
5.
Vopr Med Khim ; 31(1): 65-8, 1985.
Artigo em Russo | MEDLINE | ID: mdl-2984843

RESUMO

Activity of transport ATPases was studied in erythrocyte membranes and synaptosomal fraction of cervical department of spinal cord obtained from rats in dynamics of botulinic C intoxication Na+, K+-ATPase was inhibited by the competitive type in the synaptosomal brain fraction at the preclinical period of intoxication and by the noncompetitive type at the step of skeletal muscle paresis. In erythrocyte membranes activity of Na+, K+-ATPase was inhibited by the mixed type at the preclinical period of intoxication and the enzymatic activity was inhibited by the noncompetitive type at the step of skeletal muscle paresis. The Na+, K+-ATPase from biological membranes was reactivated by unithiol and nicotinamide in dynamics of intoxication. The toxin was shown to activate Mg2+-ATPase in brain synaptosomal fraction.


Assuntos
Adenosina Trifosfatases/antagonistas & inibidores , Toxinas Botulínicas/farmacologia , Botulismo/enzimologia , Membrana Eritrocítica/enzimologia , Membranas Sinápticas/enzimologia , Animais , ATPase de Ca(2+) e Mg(2+) , Hidrólise , Cinética , Ratos , ATPase Trocadora de Sódio-Potássio/antagonistas & inibidores , Medula Espinal/enzimologia
6.
Biull Eksp Biol Med ; 94(9): 29-31, 1982 Sep.
Artigo em Russo | MEDLINE | ID: mdl-6293618

RESUMO

The effect of type C botulinum toxin on Na, K, Mg-ATPase activities of erythrocyte membranes of white rats was studied in experiments in vivo and in vitro. The activity of Na, K, Mg-ATPase was found to be markedly inhibited in the preclinical period of poisoning, 2 hours after intraperitoneal injection of the toxin. In this case Mg-ATPase activity noticeably increased. In the presence of the development of a grave paralytic syndrome one day after intraperitoneal injection of the toxin, the activity of Na, K-ATPase of the erythrocyte membrane remained decreased as was the case in the preclinical period of poisoning, whereas the activity of Mg-ATPase returned to normal. The experiments in vitro with preincubation of erythrocyte membranes with botulinum toxin in the concentrations corresponding to the mean calculated ones in the experiments in vivo demonstrated inhibition of Na, K-ATPase. The magnitude of Mg-ATPase activity remained virtually unchanged in all the modifications of the experiments with boiled and native botulinum toxin. The in-vivo experiments with intraperitoneal injection of glutathione and unithiol to the pretreated animals attested to normalization of Na, K-ATPase in the preclinical period of poisoning, with this normalization being brought about by unithiol. In the in-vitro experiments with addition of unithiol or glutathione into the incubation medium, each of the donators of sulphhydryl groups prevented Na, K-ATPase inhibition with botulinum toxin.


Assuntos
Toxinas Botulínicas/farmacologia , Botulismo/enzimologia , Membrana Eritrocítica/enzimologia , Eritrócitos/enzimologia , ATPase Trocadora de Sódio-Potássio/sangue , Animais , Reativadores Enzimáticos , Glutationa/farmacologia , Técnicas In Vitro , Ratos , Unitiol/farmacologia
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