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Molecular gene cloning and overexpression of the phytase from Debaryomyees castellii CBS 2923 Inra
Ragon, M.; Neugnot-Roux, V.; Chemardin, P.; Moulin, G.; Boze, H..
The ORF encoding the Debaryomyces castellii CBS 2923 phytase was isolated. The deduced 461-amino-acid sequence corresponded to a 51.2 kDa protein and contained the consensus motif (RHGXRXP) which is conserved among phytases. No signal sequence cleavage site was detected. Nine potential N-glycosylation sites have been predicted. The protein shared 21-69% sequence identities with various phytases of yeast or fungal origin. Heterologous expression of the D. castellii CBS 2923 phytase in the methylotrophic yeast Pichia pastoris was tested under both the P. pastoris inducible alcohol oxidase (AOX1) promoter and the constitutive glyceraldehyde-3-phosphate dehydrogenase (GAP) promoter. Maximum production levels obtained were 476 U ml(-1), with the AOX1 expression...
Tipo: Journal Article Palavras-chave: GENE ISOLATION; PHYTASE; DEBARYOMYCES CASTELLII; PICHIA PASTORIS; HETEROLOGOUS EXPRESSION.
Ano: 2008 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2009ea2756c4&uri=/notices/prodinra1/2010/08/
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Overexpression and characterization of two human salivary proline rich proteins Inra
Pascal, C.; Bigey, F.; Ratomahenina, R.; Boze, H.; Moulin, G.; Manchado-Sarni, P..
Proline rich proteins (PRP) are among major human saliva constituents and are known to interact with wine tannins that are involved in astringency. To characterize these interactions, a human salivary proline rich pro-protein, PRB4S, was overexpressed in Pichia pastoris. Six recombinant proteins resulting from maturation in bioreactor were detected by SDS-PAGE analysis between 15 and 45 kDa (apparent molecular weight). Two of them, the 45 and the 15 kDa ones, were isolated from culture supernatant by adsorption and permeation chromatography. They were characterized by N-terminal sequencing and MALDI-TOF analysis after trypsic digestion. The 45 kDa protein is glycosylated while the 15 kDa one was obtained after a furin-like proteolysis. Both of them are...
Tipo: Journal Article Palavras-chave: HUMAN SALIVARY PRP; PRB4S; PICHIA PASTORIS; OVEREXPRESSION; TRYPSIC DIGESTION; MALDI-TOF; N-TERMINAL SEQUENCE; INTRINSICALLY UNSTRUCTUREDPROTEIN; II-1; IB-5.
Ano: 2006 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD200846b46bb&uri=/notices/prodinra1/2009/03/
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Refined solution structure of a liganded type 2 wheat nonspecific lipid transfer protein Inra
Pons, J.L.; de Lamotte, F.; Gautier, M.F.; Delsuc, M.A..
The refined structure of a wheat type 2 nonspecific lipid transfer protein (ns-LTP2) liganded withl-α-palmitoylphosphatidylglycerol has been determined by NMR. The 15N-labeled protein was produced in Pichia pastoris. Physicochemical conditions and ligandation were intensively screened to obtain the best NMR spectra quality. This ns-LTP2 is a 67-residue globular protein with a diameter of about 30 Å. The structure is composed of five helices forming a right superhelix. The protein presents an inner cavity, which has been measured at 341 Å3. All of the helices display hydrophobic side chains oriented toward the cavity. The phospholipid is found in this cavity. Its fatty acid chain is completely inserted in the protein, the l-α-palmitoylphosphatidylglycerol...
Tipo: Journal Article Palavras-chave: PROTEINE TRANSFERT DE LIPIDE; BIOCHIMIE STRUCTURALE; SPECTROSCOPIE RMN; TECHNIQUE ANALYTIQUE; PICHIA PASTORIS; STRUCTURE TRIDIMENSIONNELLE; PLANTE; SEQUENCE NUCLEOTIDIQUE; PHOSPHOLIPIDE; LIAISON.
Ano: 2003 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB0400023062101609&uri=/notices/prodinra1/2010/11/
Registros recuperados: 3
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