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Exp Parasitol ; 79(2): 99-105, Sept. 1994.
Artigo em Inglês | MedCarib | ID: med-2119


Forty-one-, 31-, and 28-kDa proteins of strongyloides stercoralis filariform larvae have previously been demonstrated to be sensitively and specifically recognized by serum IgG in individuals with strongyloidiasis. Characteristics of these proteins, their immunodominant epitopes, and reactive antibodies are described here. The proteins are soluble is aqueous as well as detergent extracts. The immunodominant epitopes are present in S. stercoralis but not in S. cebus or S. ratti. Epitopes on the three proteins are not shared, as determined by cross-absorption of serum with each of the size components on nitrocellulose. In most sera from strongyloidiasis patients there was reactivity to each of the proteins by IgG1 and IgG4, but reactivity by IgG2 or IgG3 was detectable only in a minority. A rabbit antiserum raised to a 41-kDa size fraction of S. stercoralis larvae reacted against a doublet of 41-kDa which was distinct from the immunodiagnostic 41-kDa protein.(AU)

Anticorpos Anti-Helmínticos/biossíntese , Anticorpos Anti-Helmínticos/diagnóstico , Epitopos Imunodominantes/análise , Strongyloides stercoralis/imunologia , Estrongiloidíase/diagnóstico , Anticorpos Anti-Helmínticos/sangue , Anticorpos Anti-Helmínticos/imunologia , Western Blotting , Eletroforese em Gel de Poliacrilamida , Imunoglobulina G/biossíntese , Imunoglobulina G/sangue , Soros Imunes/imunologia , Epitopos Imunodominantes/química , Epitopos Imunodominantes/imunologia , Larva/imunologia , Peso Molecular , Onchocerca/imunologia , Coelhos , Solubilidade , Especificidade da Espécie , Strongyloides ratti/imunologia , Estrongiloidíase/imunologia
Int J Leg Med ; 104(4): 221-7, 1991.
Artigo em Inglês | MedCarib | ID: med-10566


Populations of white Caucasians, Afro-Caribbeans and Asians residing within the UK have been analysed at 4 different hypervariable loci. A computerised system was used to store and to analysed the data. Simulation experiments were carried out in order to determine whether there was any evidence for population stratification, which would lead to non-independence of allelic distributions. (AU)

Humanos , /genética , /genética , /genética , Alelos , Ásia/etnologia , Medicina Legal/métodos , Reino Unido , Heterozigoto , Homozigoto , Peso Molecular , Índias Ocidentais/etnologia
Biochem Biophys Res Commun ; 40(6): 1507-13, Sept. 30, 1970.
Artigo em Inglês | MedCarib | ID: med-9248


Previous findings in the literature that rhein inhibits DPNH-linked mitochondrial oxidations by acting in the DPNH dehydrogenase region of the respiratory chain have been confirmed and extended. In the micromolar range rhein inhibits DPNH oxidase and DPNH-ferricyanide activities and the energy-linked reduction of DPNH by succinate in membrane preparations from heart, as wellas the DPNH dehydrogenase and transhydrogenase activities of the soluble, purified enzyme. The inhibition of the activities of the soluble enzyme are purely competitive with respect to substrate. These facts localize the primary inhibition site of rhein between substrate and FMN. In heart ETP a second noncompetitive inhibition is also present but is detectable only at very low (<10æM) rhein concentrations. Rhein also inhibits DPNH dehydrogenase in Candida utilis mitochondria and the purified enzyme from liver. On conversion of the heart enzyme to the low molecule weight DPNH-cytochrome reductase the typical effect of rhein disappears and is replaced by a slight stimulation or inhibition, depending on the electron acceptor used, showing that the substrate binding site is modified in this form of the enzyme. In beef liver mitochondria DPNH oxidation may appear insensitive to rhein, probably because of the strong binding of rhein to other proteins. To a lesser extent unspecific binding of rhein and resultant interference with the inhibition of DPNH dehydrogenase is also shown by BSA and by proteins in heart ETP. Rhein also inhibits transhydrogenations in mitochondria and at higher concentrations lactate and malate dehydrogenases but has no effect on sccinate, alcohol (liver nad yeast), and glucose-6-p dehydrogenases or on Neuospora DPN-ase, glucose-6-phosphatase, and amine oxidase. (SUMMARY)

Humanos , Recém-Nascido , Lactente , Adulto , Antraquinonas/farmacologia , Mitocôndrias Musculares/metabolismo , Oxirredutases/antagonistas & inibidores , Candida/enzimologia , Citocromos , Depressão Química , Transporte de Elétrons , Fibroblastos/citologia , Glucose-6-Fosfatase/antagonistas & inibidores , Glucosefosfato Desidrogenase/antagonistas & inibidores , Cinética , Membranas/enzimologia , Mitocôndrias/efeitos dos fármacos , Mitocôndrias/enzimologia , Mitocôndrias Hepáticas , Mitocôndrias Musculares/efeitos dos fármacos , Peso Molecular , Miocárdio/citologia , Neurospora/enzimologia , N-Glicosil Hidrolases/antagonistas & inibidores , NAD/metabolismo , Oxirredução , Oxirredutases/isolamento & purificação , Oxirredutases/metabolismo , Polivinil/farmacologia , Ligação Proteica , Saccharomyces/efeitos dos fármacos , Saccharomyces/enzimologia , Soroalbumina Bovina/farmacologia , Solubilidade , Ácidos Sulfúricos/farmacologia