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Registros recuperados: 9
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Characterization of isoforms of equine alpha-s1 casein: post-transcriptional variants and phosphorylation post-translational variants Inra
Matéos, A.; Miclo, L.; Mollé, D.; Girardet, J.M.; Gaillard, J.L..
Tipo: Meeting Paper Palavras-chave: LAIT DE JUMENT; HAFLINGER; MICRO-HETEROGENEITE; ALPHA-S1 CASEINE.
Ano: 2008 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2010969df608&uri=/notices/prodinra1/2011/06/
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Chymosin sensitivity of the heat-induced serum protein aggregates isolated from skim milk Inra
Mollé, D.; Jean, K.; Guyomarc'h, F..
The sensitivity of heat-induced milk serum κ-casein/whey protein aggregates to recombinant chymosin was investigated in the serum phase of heated skim milk or on aggregates isolated from it. In both cases, significant amounts of caseinomacropeptide were produced after 1 h-incubation at 37 °C, as assayed by high performance liquid chromatography coupled with mass spectrometry analysis. In milk serum, the aggregates remained stable upon hydrolysis, as opposed to 10 g L−1 suspensions of isolated aggregates in imidazole/Ca2+ buffer where visible flocculation occurred. The results are discussed in terms of variation in chymosin activity between the two systems.
Tipo: Journal Article Palavras-chave: CHYMOSINE; PROTEINE; LACTOSERUM DENATURATION; AGGREGATION; RENNETING; WHEY PROTEIN.
Ano: 2006 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2007aeb7bce5&uri=/notices/prodinra1/2007/10/
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Determination of exposed sulfhydryl groups in heated β-lactoglobulin A using IAEDANS and mass spectrometry Inra
Kehoe, J.J.; Brodkorb, A.; Mollé, D.; Yokoyama, E.; Famelart, M.H.; Bouhallab, S.; Morris, E.R.; Croguennec, T..
This paper takes a new approach to determining which sulfhydryl groups are exposed during the heat denaturation of bovine â-lactoglobulin A. The sulfhydryl groups exposed after heating wereblocked with 5-((((2-iodoacetyl)amino)ethyl)amino)naphthalene-1-sulfonic acid (IAEDANS). The results show that IAEDANS is a suitable blocking agent, and its absorbance at 336 nm enabled thequantification of exposed sulfhydryl groups in a mixture of protein species by gel permeation chromatography. Combined with the specific fragmentation of bound IAEDANS by matrix-assisted laser desorption ionization (MALDI) MS/MS in negative ionization mode, this facilitated the identificationof peptides that contained blocked cysteines after enzymatic digestion of the protein. During...
Tipo: Journal Article Palavras-chave: BOVINE BETA-LACTOGLOBULIN; MALDI MASS SPECTROMETRY; HEAT DENATURATION; IAEDANS; FREE SULFHYDRYL.
Ano: 2007 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2008f53ef5ea&uri=/notices/prodinra1/2008/04/
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New genetic variants identified in donkey's milk whey proteins Inra
Herrouin, M.; Mollé, D.; Fauquant, J.; Ballestra, F.; Maubois, J.L.; Léonil, J..
Novel genetic variants for donkey milk lysozyme and β-lactoglobulins I and II have been identified by the combined use of peptide mass mapping and sequencing by tandem mass spectrometry in association with database searching. The novel donkey lysozyme variant designated as lysozyme B (Mr 14,631 Da) differed in three amino acid exchanges, N49 -> D, Y52 -> S, and S61 -> N, from the previously published sequence. Three novel genetic variants for donkey β-lactoglobulins were identified. One of them is a typeβ-lactoglobulin I with three amino acid exchanges at E36 -> S, S97 -> T, and V150 -> I (β-lactoglobulin I B, Mr 18,510 Da). The two others are type β-lactoglobulins II with two amino acid exchanges at C110 -> P and M118 -> T...
Tipo: Journal Article Palavras-chave: TECHNOLOGIE LAITIERE; SPECTROMETRIE DE MASSE; SAUMURE; EGOUTTAGE; LYSOZYME; BETA LACTOGLOBULINE; SEQUENCE NUCLEOTIDIQUE; EQUIDAE; HPLC MASS SPECTROMETRY; PROTEIN SEQUENCE; WHEY PROTEIN; DONKEY MILK.
Ano: 2000 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB0200006707093904&uri=/notices/prodinra1/2010/12/
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Phosphorylation variants of equine beta-casein: purification of caseinophosphopeptides and determination of the phosphorylation sites Inra
Matéos, A.; Miclo, L.; Mollé, D.; Girardet, J.M.; Gaillard, J.L..
Tipo: Meeting Paper Palavras-chave: LAIT DE JUMENT; BETA-CASEIN ; CASEINO-PHOSPHOPEPTIDE; PURIFICATION.
Ano: 2008 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2010e5c561e8&uri=/notices/prodinra1/2011/06/
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Protein composition and polymorphism in the milk of Skopelos goats Inra
Moatsou, G.; Vamvakaki, A.N.; Mollé, D.; Anifantakis, E.; Léonil, J..
Des laits individuels de chèvres de Skopelos (Grèce) ont été analysés par RP-HPLC et les profils protéiques ont été comparés avec ceux issus de lait de chèvres de génotypes connus au locus as1. Les échantillons qui présentaient des caractéristiques particulières de leur fraction caséique ont été analysés par IEF et RP-HPLC/ESI-MS. Les teneurs moyennes en protéines totales (36,7 ± 2,6 g·L-1), et en caséines (29,7 ± 2,3 g·L-1), étaient plus élevées que dans les laits des races hautement sélectionnées. Le pourcentage en as1-cn représentait 21,8 % des caséines totales, tandis que celui de la b-cn atteignait 43,8 %. Les pourcentages en as2-cn et k-cn étaient respectivement 13,7 % et 13,8 %. Ces caractéristiques quantitatives étaient corrélées avec la...
Tipo: Journal Article Palavras-chave: POLYMORPHISME; VARIANT PROTEIQUE; LAIT DE CHEVRE GOAT MILK PROTEIN; CASEIN GENOTYPE; PHOSPHORYLATION; POLYMORPHISM.
Ano: 2006 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD200773c79f65&uri=/notices/prodinra1/2008/02/
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Proteomic analysis of hen egg white Inra
Guérin-Dubiard, C.; Pasco, M.; Mollé, D.; Désert, C.; Croguennec, T.; Nau, F..
Hen egg white is an original biological fluid in which major proteins have been widely studied, unlike the minor components. In this study, two-dimensional electrophoresis associated with mass spectrometry enabled the separation of 69 protein spots and their matching with major proteins, which were already known, and with minor proteins. Sixteen proteins were identified, and among them, two had never been previously detected in hen egg white, i.e., Tenp, a protein with strong homology with a bacterial permeability-increasing protein family (BPI), and VMO-1, an outer layer vitelline membrane protein. Thirteen proteins present a very wide polymorphism (ovotransferrin, ovomucoid, clusterin, etc.), some of them up to nine isoforms (ovoinhibitor). Eleven...
Tipo: Journal Article Palavras-chave: PROTEOME; HEN EGG WHITE PROTEIN; PEPTIDE MASS FINGERPRINTING; PEPTIDE SEQUENCING; TWO-DIMENSIONAL GEL ELECTROPHORESIS; MASS SPECTROMETRY.
Ano: 2006 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2007d0f430dc&uri=/notices/prodinra1/2008/01/
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Secretome analysis of Phanerochaete chrysosporium strains CIRM-BRFM41 grown on softwood Inra
Ravalason, H.; Jan, G.; Mollé, D.; Pasco, M.; Coutinho, P.M.; Lapierre, C.; Pollet, B.; Bertaud, F.; Petit-Conil, M.; Grisel, S.; Sigoillot, J.C.; Asther, M.; Gimbert, I..
Abstract Proteomic analysis was performed to determine and differentiate the composition of the secretomes of Phanerochaete chrysosporium CIRM-BRFM41, a peroxidasehypersecretory strain grown under ligninolytic conditions and on softwood chips under biopulping conditions.Extracellular proteins from both cultures were analyzed by bidimensional gel electrophoresis and matrix-assisted laserdesorption/ionization time-of-flight tandem mass spectrometry.A total of 37 spots were identified. The secretome in liquid synthetic medium comprised mainly peroxidases,while several wood-degrading enzymes and enzymes involved in fungal metabolism were detected in biopulping cultures on softwood. This prompted an analysis of the impact of secretome modulation in the presence...
Tipo: Journal Article Palavras-chave:  SECRETOME SOFTWOOD CHEMICAL PULPING; Phanerochaete chrysosporium.
Ano: 2008 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD20092bd81e9f&uri=/notices/prodinra1/2010/09/
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Study of caprine ß-casein using reversed-phase high-performance liquid chromatography and mass spectrometry: Identification of a new genetic variant Inra
Moatsou, G.; Mollé, D.; Moschopoulou, E.; Gagnaire, N..
The genotypes and the main phosphorylationlevels of b-casein of goat milk were studied using RPHPLC/ ESI-MS. A new variant of caprine b-casein named E has been characterized using RP-HPLC/ESI-MS,MALDI-MS and NanoESI MS/MS methods. Its sequence differed from that of variant A in the mono amino acid substitution D47 ? Y47, which resulted in a 48 Da experimental mass difference between them. The calculatedmolecular mass of the new variant E 6 P wasestimated as 23,869 Da. Its phosphorylation pattern was similar to that of variant A, the most abundant types being those with 5 and 6 P in similar quantities.
Tipo: Journal Article Palavras-chave: BETA-CASEIN; CHROMATOGRAPHY HPLC; MASS SPECTROSCOPY; IDENTIFICATION; GOAT MILK; POLYMORPHISME; GENETIC VARIANT; POLYMORPHISM.
Ano: 2007 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD20087f93f240&uri=/notices/prodinra1/2008/04/
Registros recuperados: 9
Primeira ... 1 ... Última
 

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