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| 49. |  | MICLO, L.; GIRARDET, J. -M.; EGITO, A. S. do; MOLLÉ, D.; MARTIN, P.; GAILLARD, J. L. The primary structure of a low-M(r) multiphosphorylated variant of beta-casein in equine milk. Proteomics, v. 7, n. 8, p. 1327-1335, Mar. 2007.| Biblioteca(s): Embrapa Caprinos e Ovinos. |
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| 59. | | LAGUNA, L. E.; EGITO, A. S. do; NUNES, R. G. F. Avaliação físico-química do leite de cabra em três rebanhos mestiços na região de Sobral, Ceará, Brasil. Revista do Instituto de Laticínios Cândido Tostes, Juiz de Fora, v. 53, n. 304, p. 153-157, 1998. Edição dos Anais do XV Congresso Nacional de Laticínios, Juiz de Fora, 1998.| Biblioteca(s): Embrapa Caprinos e Ovinos. |
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| 60. | | EGITO, A. S. do; NUNES, R. G. F.; LAGUNA, L. E.; ARAUJO, A. M. de. Características físico-químicas do leite de cabra produzido na região de Sobral, Ceará. In: CONGRESSO BRASILEIRO DE MEDICINA VETERINÁRIA, 25.; CONGRESSO DE MEDICINA VETERINÁRIA DO CONE SUL, 2.; CONGRESSO ESTADUAL DE MEDICINA VETERINÁRIA, 13., 1997, Gramado, RS. "A integração cientifica da medicina veterinária no Cone Sul": anais. Porto Alegre: Sociedade de Veterinária do Rio Grande do Sul, 1997. p. 301. Res. ITA-020.| Biblioteca(s): Embrapa Caprinos e Ovinos. |
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 | Acesso ao texto completo restrito à biblioteca da Embrapa Caprinos e Ovinos. Para informações adicionais entre em contato com cnpc.biblioteca@embrapa.br. |
Registro Completo
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Biblioteca(s): |
Embrapa Caprinos e Ovinos. |
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Data corrente: |
29/02/2008 |
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Data da última atualização: |
25/09/2019 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Circulação/Nível: |
Internacional - A |
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Autoria: |
MICLO, L.; GIRARDET, J. -M.; EGITO, A. S. do; MOLLÉ, D.; MARTIN, P.; GAILLARD, J. L. |
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Afiliação: |
Miclo L, Unité de Recherche sur l'Animal et les Fonctionnalités des Produits Animaux (UR AFPA L'Institut National de la Recherche Agronomique (INRA); Girardet J. M., Unité de Recherche sur l'Animal et les Fonctionnalités des Produits Animaux (UR AFPA L'Institut National de la Recherche Agronomique (INRA); ANTONIO SILVIO DO EGITO, CNPC; Mollé D, L'Institut National de la Recherche Agronomique; Martin P., Unité Génomique et Physiologie de la Lactation (GLP) Institut National de la Recherche Agronomique; Gaillard J. L., Unité de Recherche sur l'Animal et les Fonctionnalités des Produits Animaux (UR AFPA L'Institut National de la Recherche Agronomique (INRA). |
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Título: |
The primary structure of a low-M(r) multiphosphorylated variant of beta-casein in equine milk. |
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Ano de publicação: |
2007 |
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Fonte/Imprenta: |
Proteomics, v. 7, n. 8, p. 1327-1335, Mar. 2007. |
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Idioma: |
Inglês |
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Conteúdo: |
Highly phosphorylated casein with a low molecular mass was isolated from Haflinger mare's milk by RP-HPLC. It accounts for 4.0% of the casein content. Its mass was determined by LC-ESI-MS before and after treatment by alkaline phosphatase. The molecular mass found for the apo-form (10 591 ± 2 Da) is in agreement with its primary structure, which was established by ESI-MS/MS from tryptic peptides. It appeared that this short protein (94 amino acid residues) is an internally truncated form of the full-length equine -casein (226 residues). This low-Mr variant of equine -casein displays a large deletion (residues 50-181), due to a cryptic splice site usage occurring within exon 7 during the course of primary transcripts processing. The phosphorylation pattern of this equine -casein variant was investigated by LC-ESI-MS and 2-DE. Seven phosphorylation forms were identified with one to seven phosphate groups with pIs ranging between 4.67 and 4.01. The major isoforms carry five and six phosphate groups. |
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Palavras-Chave: |
Equine Milk; Fosforização; High Pressure Liquid; Leite de égua. |
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Thesagro: |
Caseína; Enzima. |
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Thesaurus NAL: |
Alternative splicing; Amino acid sequences; Beta-casein; Chromatography; Food chemistry; Gel electrophoresis; Horses; Mass spectrometry; Peptides; Phosphorylation; Protein isoforms. |
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Categoria do assunto: |
L Ciência Animal e Produtos de Origem Animal |
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Marc: |
LEADER 02070naa a2200385 a 4500
001 1521814
005 2019-09-25
008 2007 bl uuuu u00u1 u #d
100 1 $aMICLO, L.
245 $aThe primary structure of a low-M(r) multiphosphorylated variant of beta-casein in equine milk.$h[electronic resource]
260 $c2007
520 $aHighly phosphorylated casein with a low molecular mass was isolated from Haflinger mare's milk by RP-HPLC. It accounts for 4.0% of the casein content. Its mass was determined by LC-ESI-MS before and after treatment by alkaline phosphatase. The molecular mass found for the apo-form (10 591 ± 2 Da) is in agreement with its primary structure, which was established by ESI-MS/MS from tryptic peptides. It appeared that this short protein (94 amino acid residues) is an internally truncated form of the full-length equine -casein (226 residues). This low-Mr variant of equine -casein displays a large deletion (residues 50-181), due to a cryptic splice site usage occurring within exon 7 during the course of primary transcripts processing. The phosphorylation pattern of this equine -casein variant was investigated by LC-ESI-MS and 2-DE. Seven phosphorylation forms were identified with one to seven phosphate groups with pIs ranging between 4.67 and 4.01. The major isoforms carry five and six phosphate groups.
650 $aAlternative splicing
650 $aAmino acid sequences
650 $aBeta-casein
650 $aChromatography
650 $aFood chemistry
650 $aGel electrophoresis
650 $aHorses
650 $aMass spectrometry
650 $aPeptides
650 $aPhosphorylation
650 $aProtein isoforms
650 $aCaseína
650 $aEnzima
653 $aEquine Milk
653 $aFosforização
653 $aHigh Pressure Liquid
653 $aLeite de égua
700 1 $aGIRARDET, J. -M.
700 1 $aEGITO, A. S. do
700 1 $aMOLLÉ, D.
700 1 $aMARTIN, P.
700 1 $aGAILLARD, J. L.
773 $tProteomics$gv. 7, n. 8, p. 1327-1335, Mar. 2007.
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