Potato Apyrase
Mostrando 1-9 de 9 artigos, teses e dissertações.
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1. IgE antibodies from schistosomiasis patients to recognize epitopes in potato apyrase
Abstract INTRODUCTION: High percentages of structural identity and cross-immunoreactivity have been reported between potato apyrase and Schistosoma mansoni ATP diphosphohydrolase (SmATPDases) isoforms, showing the existence of particular epitopes shared between these proteins. METHODS: Potato apyrase was employed using ELISA, western blot, and mouse immu
Rev. Soc. Bras. Med. Trop.. Publicado em: 28/03/2019
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2. Immunostimulatory property of a synthetic peptide belonging to the soluble ATP diphosphohydro-lase isoform (SmATPDase 2) and immunolocalisation of this protein in the Schistosoma mansoni egg
A peptide (SmB2LJ; r175-194) that belongs to a conserved domain from Schistosoma mansoni SmATPDase 2 and is shared with potato apyrase, as predicted by in silico analysis as antigenic, was synthesised and its immunostimulatory property was analysed. When inoculated in BALB/c mice, this peptide induced high levels of SmB2LJ-specific IgG1 and IgG2a subtypes, a
Memórias do Instituto Oswaldo Cruz. Publicado em: 2011-11
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3. Identificação de um domínio conservado e antigênico de ATP difosfohidrolases de parasitos, também presente em uma isoforma ativa de Leishmania (Leishmania) chagasi
Através do alinhamento de sequências de aminoácidos, análise filogenética e predição de peptídeos, nós demonstramos uma relação evolucionária e estreita relação estrutural entre um domínio particular da apirase de batata e várias proteínas de organismos patogênicos, todos eles pertencentes à família das ATP difosfohidrolases. Um fragmento
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 01/10/2010
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4. Identificação de alvos antigênicos na ATP difosfohidrolase solúvel de Schistosoma mansoni e possível aplicação funcional de peptídeos sintéticos
The antigenicity of both soluble S. mansoni ATP diphosphohydrolase and membraneassociated isoforms has been recently described. Cross-immunoreactivity between potato apyrase and IgG antibody from S. mansoni-infected mice or schistosomiasis patients strongly suggested that the epitopes shared between the vegetable and parasite proteins are antigenic. By bioin
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 02/06/2010
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5. Antibody reactivity against potato apyrase, a protein that shares epitopes with Schistosoma mansoni ATP diphosphohydrolase isoforms, in acute and chronically infected mice, after chemotherapy and reinfection
Schistosoma mansoni ATP diphosphohydrolase isoforms and potato apyrase share conserved epitopes. By enzyme-linked immunosorbent assays, elevated levels of IgM, IgG2a and IgG1 antibody reactivity against potato apyrase were observed in S. mansoni-infected BALB/c mice during the acute phase of infection, while only IgM and IgG1 antibody reactivity levels maint
Memórias do Instituto Oswaldo Cruz. Publicado em: 2010-07
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6. Detection of IgG1 and IgG4 subtypes reactive against potato apyrase in schistosomiasis patients
In this paper, we showed for the first time that the conserved domains within Schistosoma mansoni ATP diphosphohydrolase isoforms, shared with potato apyrase, possess epitopes for the IgG1 and IgG4 subtypes, as 24 (80%) of the 30 schistosomiasis patients were seropositive for this vegetable protein. The analyses for each patient cured (n = 14) after treatmen
Memórias do Instituto Oswaldo Cruz. Publicado em: 2010-07
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7. Cross-immunoreactivity between anti-potato apyrase antibodies and mammalian ATP diphosphohydrolases: potential use of the vegetal protein in experimental schistosomiasis
We have previously showed that Schistosoma mansoni ATP-diphosphohydrolase and Solanum tuberosum potato apyrase share epitopes and the vegetable protein has immunostimulatory properties. Here, it was verified the in situ cross-immunoreactivity between mice NTPDases and anti-potato apyrase antibodies produced in rabbits, using confocal microscopy. Liver sample
Memórias do Instituto Oswaldo Cruz. Publicado em: 2006-10
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8. Studies on ATP-diphosphohydrolase nucleotide-binding sites by intrinsic fluorescence
Potato apyrase, a soluble ATP-diphosphohydrolase, was purified to homogeneity from several clonal varieties of Solanum tuberosum. Depending on the source of the enzyme, differences in kinetic and physicochemical properties have been described, which cannot be explained by the amino acid residues present in the active site. In order to understand the differen
Brazilian Journal of Medical and Biological Research. Publicado em: 2000-07
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9. Regulation of Plant Pyruvate Dehydrogenase Complex by Phosphorylation 1
The ATP-dependent inactivation of the pyruvate dehydrogenase complex (PDC) was examined using ruptured mitochondria and partially purified pyruvate dehydrogenase complex isolated from broccoli and cauliflower (Brassica oleracea) bud mitochondria. The ATP-dependent inactivation was temperature- and pH-dependent. [32P]ATP experiments show a specific transphosp