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.
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Registro original: |
Embrapa Caprinos e Ovinos (CNPC) |
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