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Registros recuperados: 4
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Complete hydrolysis of myo-inositol hexakisphosphate by a novel phytase from Debaryomyces castellii CBS 2923 Inra
Ragon, M.; Aumelas, A.; Chemardin, P.; Galvez, S.; Moulin, G.; Boze, H..
Debaryomyces castellii phytase was purified to homogeneity in a single step by hydrophobic interaction chromatography. Its molecular mass is 74 kDa with 28.8% glycosylation. Its activity was optimal at 60 C and pH 4.0. The Km value for sodium phytate was 0.532 mM. The enzyme exhibited a low specificity and hydrolyzed many phosphate esters. The phytase fully hydrolyzed myo-inositol hexakisphosphate ( or phytic acid, Ins P-6) to inositol and inorganic phosphate. The sequence of Ins P-6 hydrolysis was determined by combining results from high-performance ionic chromatography and nuclear magnetic resonance. D. castellii phytase is a 3-phytase that sequentially releases phosphate groups through Ins ( 1,2,4,5,6) P-5, Ins ( 1,2,5,6) P-4, Ins ( 1,2,6) P-3, Ins (...
Tipo: Journal Article Palavras-chave: DEBAROMYCES CASTELLII; YEAST; PHYTASE; ENZYME CHARACTERIZATION; INOSITOL PHOSPHATE; PHYTATE DEGRADATION; NMR; HPLC.
Ano: 2008 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2009150d6498&uri=/notices/prodinra1/2010/09/
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NMR structure of rALF-Pm3, an anti-lipopolysaccharide factor from shrimp: model of the possible lipid A-binding site Inra
Yang, Y.; Boze, H.; Chemardin, P.; Padilla, A.; Moulin, G.; Tassanakajon, A.; Pugnière, M.; Roquet, F.; Destoumieux-Garzon, D.; Gueguen, Y.; Bachère, E.; Aumelas, A..
The anti-lipopolysaccharide factor ALF-Pm3 is a 98-residue protein identified in hemocytes from the black tiger shrimp Penaeus monodon. It was expressed in Pichia pastoris from the constitutive glyceraldehyde-3-phosphate dehydrogenase promoter as a folded and N-15 uniformly labeled rALF-Pm3 protein. Its 3D structure was established by NMR and consists of three alpha-helices packed against a four-stranded beta-sheet. The C-34-C-55 disulfide bond was shown to be essential for the structure stability. By using surface plasmon resonance, we demonstrated that rALF-Pm3 binds to LPS, lipid A and to OM(R)-174, a soluble analogue of lipid A. Biophysical studies of rALF-Pm3/LPS and rALF-Pm3/OM(R)-174 complexes indicated rather high molecular sized aggregates, which...
Tipo: Journal Article Palavras-chave: ANTI-LIPOPOLYSACCHARIDE FACTOR ; LIPOPOLYSACCHARIDE; LIPID A; NMR; STRUCTURE; SEPTIC SHOCK; SURFACE PLASMON RESONANCE ULTRACENTRIFUGATION.
Ano: 2009 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD201064bb8a78&uri=/notices/prodinra1/2010/09/
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Production of an Arabidopsis halleri foliar defensin in Escherichia coli Inra
Marquès, L.; Oomen, R.; Aumelas, A.; Le Jean, M.; Berthomieu, P..
Production of the recombinant Arabidopsis halleri defensin AhPDF1.1 in a native-like form. Mature AhPDF1.1 cDNA was cloned into pET-28-a(+) and expressed in Escherichia coli Rosetta. After a denaturing extraction, purification by metal affinity chromatography and CNBr cleavage of the His-tag, a protein without extra amino acids at the N-terminus was obtained. An oxidative folding step was then required to renature the protein that was then purified to homogeneity by a C18 HPLC separation. Mass spectroscopy and circular dichroism analyses showed that the recombinant AhPDF1.1 has the expected molecular mass and 3D-structure features of a folded defensin with four-disulfide bridges. The recombinant protein is active against the filamentous fungus Fusarium...
Tipo: Journal Article Palavras-chave: ARABIDOPSIS HALLERI; CNBR CLEAVAGE; NATIVE-LIKE PROTEIN; PLANT DEFENSIN; RECOMBINANT AHPDF1.1.
Ano: 2009 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2010699df61f&uri=/notices/prodinra1/2010/12/
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Recombinant expression and anti-microbial activity of anti-lipopolysaccharide factor (ALF) from the black tiger shrimp Penaeus monodon Inra
Somboonwiwat, K.; Marcos, M.; Tassanakajon, A.; Klinbunga, S.; Aumelas, A.; Romestand, B.; Gueguen, Y.; Boze, H.; Moulin, G.; Bachère, E..
Anti-lipopolysaccharide factors (ALFs), originally characterized from horseshoe crabs, have been recently identified from hemocytes of the black tiger shrimp, Penaeus monodon, by a genomic approach. In order to characterize the properties and biological activities of this immune effector in shrimp, ALFPm3, the most abundant isoform found in P. monodon, was expressed in the yeast Pichia pastoris. Large-scale production in fermentor provided 262 mg/l of recombinant ALFPm3 which was purified to homogeneity by single chromatography step on expanded-bed Streamline SP6XL. The rALFPm3 was further characterized in terms of N-terminal sequencing and mass spectrometry. Anti-microbial assays demonstrated that rALFPm3 has a broad spectrum of anti-fungal properties...
Tipo: Journal Article Palavras-chave: SHRIMP; CRUSTACEAN; ANTI-LIPOPOLYSACCHARIDE FACTOR; LPS-BINDING; ANTI6mICROBIAL ACTIVITY; VIBRIO; HEMOCYTE.
Ano: 2005 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD20092e49f543&uri=/notices/prodinra1/2010/10/
Registros recuperados: 4
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