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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. |
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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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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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Registro original: |
Embrapa Caprinos e Ovinos (CNPC) |
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| Acesso ao texto completo restrito à biblioteca da Embrapa Gado de Leite. Para informações adicionais entre em contato com cnpgl.biblioteca@embrapa.br. |
Registro Completo
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Biblioteca(s): |
Embrapa Gado de Leite. |
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Data corrente: |
04/04/2011 |
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Data da última atualização: |
26/03/2024 |
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Tipo da produção científica: |
Artigo de Divulgação na Mídia |
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Autoria: |
BRITO, M. A. V. P. e. |
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Afiliação: |
MARIA APARECIDA V PAIVA E BRITO, CNPGL. |
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Título: |
A qualidade do leite. |
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Ano de publicação: |
2010 |
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Fonte/Imprenta: |
Calendário DPA 2010, Goiânia, 2010. |
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Idioma: |
Português |
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Thesagro: |
Leite. |
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Categoria do assunto: |
Q Alimentos e Nutrição Humana |
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Marc: |
LEADER 00295nam a2200109 a 4500
001 1884888
005 2024-03-26
008 2010 bl uuuu u00u1 u #d
100 1 $aBRITO, M. A. V. P. e
245 $aA qualidade do leite.$h[electronic resource]
260 $aCalendário DPA 2010, Goiânia$c2010
650 $aLeite
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Embrapa Gado de Leite (CNPGL) |
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