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Registros recuperados: 6
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Identification, expression and characterization of the recombinant Sol g 4.1 protein from the venom of the tropical fire ant Solenopsis geminata J. Venom. Anim. Toxins incl. Trop. Dis.
Srisong,Hathairat; Sukprasert,Sophida; Klaynongsruang,Sompong; Daduang,Jureerut; Daduang,Sakda.
Abstract Background: Fire ant venom is a complex mixture consisting of basic piperidine alkaloids, various biologically active peptides and protein components, including a variety of major allergenic proteins. Tropical fire ant Solenopsis geminata is an important stinging ant species that causes anaphylaxis and serious medical problems. Although the biological activities of allergenic venom proteins that are unique to ant venom, particularly Solenopsis 2 and 4, are still unknown, these proteins are believed to play important roles in mediating the effects of the piperidine derivatives in the venom. Methods: In the present study, the cDNA cloning, sequencing and three-dimensional structure of Sol g 4.1 venom protein are described. The recombinant Sol g...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Fire ant; Sol g 4.1 protein; Allergen; Venom protein; Stinging ant.
Ano: 2018 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992018000100314
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Identification of LincRNA from Dermatophagoides farinae (Acari: Pyroglyphidae) for Potential Allergen-Related Targets Genet. Mol. Biol.
Zhou,Ying; Wu,Meili; Zhu,Hanting; Shao,Junjie; Liu,Chang; Cui,Yubao.
Abstract Long noncoding RNAs (lncRNAs), especially their important subclass of long intergenic noncoding RNAs (lincRNAs), have been identified in some insects. They play important roles in the regulation of biological processes, such as immune response or cell differentiation and as possible evolutionary precursors for protein coding genes. House dust mites (HDMs) are recognized as allergenic mites because allergens are found in their feces and bodies. Dermatophagoides farinae is one of the most important pyroglyphid mites because of its abundance in the household. To determine if lincRNAs can regulate allergen presentation in HDMs, we analyzed RNA-seq data for HDMs. We identified 11 lincRNAs that are related to mRNAs coding for allergens in HDMs. Using...
Tipo: Info:eu-repo/semantics/article Palavras-chave: House dust mites (HDMs); Dermatophagoides farinae; Long noncoding RNAs (lncRNAs); Allergen; RNA-seq.
Ano: 2020 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572020000100804
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Improvement of bovine ß-lactoglobulin production and secretion by Lactococcus lactis BJMBR
Nouaille,S.; Bermúdez-Humarán,L.G.; Adel-Patient,K.; Commissaire,J.; Gruss,A.; Wal,J.M.; Azevedo,V.; Langella,P.; Chatel,J.M..
The stabilizing effects of staphylococcal nuclease (Nuc) and of a synthetic propeptide (LEISSTCDA, hereafter called LEISS) on the production of a model food allergen, bovine ß-lactoglobulin (BLG), in Lactococcus lactis were investigated. The fusion of Nuc to BLG (Nuc-BLG) results in higher production and secretion of the hybrid protein. When LEISS was fused to BLG, the production of the resulting protein LEISS-BLG was only slightly improved compared to the one obtained with Nuc-BLG. However, the secretion of LEISS-BLG was dramatically enhanced (~10- and 4-fold higher than BLG and Nuc-BLG, respectively). Finally, the fusion of LEISS to Nuc-BLG resulting in the protein LEISS-Nuc-BLG led to the highest production of the hybrid protein, estimated at ~8 µg/ml...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Lactococcus lactis; Protein secretion; LEISSTCDA; Staphylococcal nuclease; SS-lactoglobulin; Allergen.
Ano: 2005 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005000300005
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Modeling of allergen proteins found in sea food products Ciênc. Tecnol. Aliment.
Galán-Freyle,Nataly; Olivero-Verbel,Jesús; Díaz-López,Liney.
Shellfish are a source of food allergens, and their consumption is the cause of severe allergic reactions in humans. Tropomyosins, a family of muscle proteins, have been identified as the major allergens in shellfish and mollusks species. Nevertheless, few experimentally determined three-dimensional structures are available in the Protein Data Base (PDB). In this study, 3D models of several homologous of tropomyosins present in marine shellfish and mollusk species (Chaf 1, Met e1, Hom a1, Per v1, and Pen a1) were constructed, validated, and their immunoglobulin E binding epitopes were identified using bioinformatics tools. All protein models for these allergens consisted of long alpha-helices. Chaf 1, Met e1, and Hom a1 had six conserved regions with...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Tropomyosin; IgE cross-reactivities; Allergen.
Ano: 2012 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612012000200028
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Production and characterization of a monoclonal antibody against an Ascaris suum allergenic component BJMBR
Pires,R.R.; Oshiro,T.M.; Itami,D.M.; Fernandes,I.; Macedo-Soares,M.F..
Ascaris suum allergenic components (PIII) separated by gel filtration chromatography of an adult worm extract were used to immunize BALB/c mice. Popliteal lymph node cells taken from the immunized animals were fused with SP2/O myeloma cells using polyethylene glycol (MW 1450) as fusogen. The hybridomas were cultured in HAT-containing medium and cloned at limiting dilutions. Supernatants from the growing hybrids were screened by ELISA using plates coated with PIII or the A. suum crude extract. The monoclonal antibody obtained, named MAC-3 (mouse anti-A. suum allergenic component), is an IgG1 kappa mouse immunoglobulin that specifically recognizes a 29,000 molecular weight protein (called allergenic protein) with an affinity constant of 1.7 x 10(9) M-1. The...
Tipo: Info:eu-repo/semantics/other Palavras-chave: Ascaris suum; Allergen; IgE; Monoclonal antibodies.
Ano: 2001 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2001000800009
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VIS/NIR spectral signature for the Identification of Peanut Contamination of Powder Foods CIGR Journal
Ghosh, Satyabrata; Domínguez, Teresa R. Cuadrado; Diezma, Belén; Lleó, Lourdes; Barreiro, Pilar; Lacarra, Teresa García; Roger, Jean-Michel.
Visible-Near Infrared reflectance spectra are proposed for the characterization IRMM 481 peanuts in comparison to powder food materials: wheat flour, milk and cocoa. Multidimensional analysis of spectra of powder samples shows a specific NIR band centred at 1200 nm that identifies peanut compared to the rest of food ingredients, regardless compaction level and temperature. Spectral range 400-1000 nm is not robust for identification of blanched peanut. The visible range has shown to be reliable for the identification of pre-treatment and processing of unknown commercial peanut samples. A spectral index is proposed based on the combination of three wavelengths around 1200 nm that is 100% robust against pre-treatment (raw or blanched) and roasting (various...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Adulterant; Food analysis; Food composition; Food quality; Allergen; PCA; Spectroscopy.
Ano: 2015 URL: http://www.cigrjournal.org/index.php/Ejounral/article/view/3216
Registros recuperados: 6
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