| |
|
|
 | 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 |
|
Biblioteca(s): |
Embrapa Caprinos e Ovinos. |
|
Data corrente: |
20/05/2008 |
|
Data da última atualização: |
25/09/2019 |
|
Tipo da produção científica: |
Artigo em Periódico Indexado |
|
Autoria: |
GIRARDET, J. -M.; N'NEGUE, M. -A.; EGITO, A. S. do; CAMPAGNA, S.; LAGRANGE, A.; GAILLARD, J. -L. |
|
Afiliação: |
Jean-Michel Girardet, Laboratoire des BioSciences de l'Aliment, Faculté des Sciences et Technique, Université Henri Poincaré-Nancy, USC, INRA, France; ANTONIO SILVIO DO EGITO, CNPC. |
|
Título: |
Multiple forms of equine a-lactalbumin: evidence for N-glycosylated and deamidated forms. |
|
Ano de publicação: |
2004 |
|
Fonte/Imprenta: |
International Dairy Journal, v. 14, n. 3, p. 207-217, Mar., 2004. |
|
Idioma: |
Inglês |
|
Conteúdo: |
Equine raw milk whey proteins were separated by anion-exchange fast protein liquid chromatography and characterised by alkaline polyacrylamide gel electrophoresis (PAGE), sodium dodecyl sulphate PAGE, and bi-dimensional PAGE. Approximately, 1% of a-lactalbumin (a-LA) was N-glycosylated. A minor N-glycosylated form of lysozyme was also found in equine milk. On the other hand, two non-glycosylated a-LA isoforms with similar molecular masses (14,21574 Da) were shown to be present. Their respective apparent isoelectric points were 5.25 and 4.94. These isoforms did not correspond to different genetic variants and were not the result of a-LA modulation by calcium ions. They corresponded rather to a non-enzymatic deamidation process of a single asparagine side-chain, the most acidic isoform being spontaneously generated from the less acidic isoform by simple incubation of a-LA at 37C. The initial rate of this chemical degradation was 4.5 mm ammonia liberated per hour, in 150mm sodium phosphate buffer pH 7.4 at 37C. Deamidation induced a slight variation in secondary structure content, but no significant change in the tertiary structure of the equine a-LA was studied by circular dichroism in the near- and far-UV regions. |
|
Palavras-Chave: |
Leite de égua; Lisosima Eletroforese bidimensional. |
|
Categoria do assunto: |
-- |
|
Marc: |
LEADER 01874naa a2200205 a 4500
001 1534014
005 2019-09-25
008 2004 bl uuuu u00u1 u #d
100 1 $aGIRARDET, J. -M.
245 $aMultiple forms of equine a-lactalbumin$bevidence for N-glycosylated and deamidated forms.$h[electronic resource]
260 $c2004
520 $aEquine raw milk whey proteins were separated by anion-exchange fast protein liquid chromatography and characterised by alkaline polyacrylamide gel electrophoresis (PAGE), sodium dodecyl sulphate PAGE, and bi-dimensional PAGE. Approximately, 1% of a-lactalbumin (a-LA) was N-glycosylated. A minor N-glycosylated form of lysozyme was also found in equine milk. On the other hand, two non-glycosylated a-LA isoforms with similar molecular masses (14,21574 Da) were shown to be present. Their respective apparent isoelectric points were 5.25 and 4.94. These isoforms did not correspond to different genetic variants and were not the result of a-LA modulation by calcium ions. They corresponded rather to a non-enzymatic deamidation process of a single asparagine side-chain, the most acidic isoform being spontaneously generated from the less acidic isoform by simple incubation of a-LA at 37C. The initial rate of this chemical degradation was 4.5 mm ammonia liberated per hour, in 150mm sodium phosphate buffer pH 7.4 at 37C. Deamidation induced a slight variation in secondary structure content, but no significant change in the tertiary structure of the equine a-LA was studied by circular dichroism in the near- and far-UV regions.
653 $aLeite de égua
653 $aLisosima Eletroforese bidimensional
700 1 $aN'NEGUE, M. -A.
700 1 $aEGITO, A. S. do
700 1 $aCAMPAGNA, S.
700 1 $aLAGRANGE, A.
700 1 $aGAILLARD, J. -L.
773 $tInternational Dairy Journal$gv. 14, n. 3, p. 207-217, Mar., 2004.
Download
Esconder MarcMostrar Marc Completo |
|
Registro original: |
Embrapa Caprinos e Ovinos (CNPC) |
|
|
Biblioteca |
ID |
Origem |
Tipo/Formato |
Classificação |
Cutter |
Registro |
Volume |
Status |
URL |
Voltar
|
|
|
| Registros recuperados : 5 | |
| 1. |  | EGITO, A. S. do; MICLO, L.; HAUSSARD, M.; POIRSON, C.; GIRARDET, J. M.; GAILLARD, J. L. Identificação de peptídeos de caseínas do leite de égua com atividade anti-hipertensiva. In: CONGRESSO BRASILEIRO DE MEDICINA VETERINÁRIA, 29., 2002, Gramado, RS. Saúde ambiental, animal e humana: uma questão de sobrevivência: anais. Gramado: Sociedade Brasileira de Medicina Veterinária, 2002. 1 CD ROM.| Tipo: Artigo em Anais de Congresso |
| Biblioteca(s): Embrapa Caprinos e Ovinos. |
|   |
| 3. | | 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.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: Internacional - A |
| Biblioteca(s): Embrapa Caprinos e Ovinos. |
|  |
| 4. | | GIRARDET, J. -M.; N'NEGUE, M. -A.; EGITO, A. S. do; CAMPAGNA, S.; LAGRANGE, A.; GAILLARD, J. -L. Multiple forms of equine a-lactalbumin: evidence for N-glycosylated and deamidated forms. International Dairy Journal, v. 14, n. 3, p. 207-217, Mar., 2004.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: Internacional - A |
| Biblioteca(s): Embrapa Caprinos e Ovinos. |
| |
| 5. | | EGITO, A. S. do; GIRARDET, J. -M.; LAGUNA, L. E.; POIRSON, C.; MOLLÉ, D.; MICLO, L.; HUMBERT, G.; GAILLARD, J. -L. Milk-clotting activity of enzyme extracts from sunflower and albizia seeds and specific hydrolysis of bovine k-casein. International Dairy Journal, v. 17, n. 7, p. 816-825, Jul. 2007.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: Internacional - A |
| Biblioteca(s): Embrapa Caprinos e Ovinos. |
| |
| Registros recuperados : 5 | |
|
| Nenhum registro encontrado para a expressão de busca informada. |
|
|
