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Registro Completo |
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Biblioteca(s): |
Embrapa Caprinos e Ovinos. |
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Data corrente: |
13/04/2018 |
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Data da última atualização: |
29/01/2024 |
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Autoria: |
JAVIER MORENO, F.; RECIO, I.; OLANO, A.; LÓPEZ-FANDIÑO, R. |
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Título: |
Chromatographic characterization of ovine kappa-casein macropeptide. |
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Ano de publicação: |
2000 |
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Fonte/Imprenta: |
Journal of Dairy Research, v. 6, n. 3, p. 349-359, Aug. 2000. |
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Idioma: |
Inglês |
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Conteúdo: |
Abstract: Ovine casein macropeptide (CMP) was characterized by anion-exchange FPLC and reversed-phase (RP) HPLC. To study heterogeneity (the degree of glycosylation and phosphorylation), CMP was desialylated with neuraminidase and dephosphorylated with acid phosphatase. Following RP-HPLC, the main CMP components were identified using either on-line or off-line mass spectrometry. The most abundant ovine CMP component was a diphosphorylated carbohydrate-free form, followed by one or two monophosphorylated and a non-phosphorylated asialo-aglyco species. Aglyco non-phosphorylated, monophosphorylated and diphosphorylated forms were in the ratio 3[ratio ]20[ratio ]77. Only ? 30% of ovine CMP was glycosylated. Assuming that the monosaccharide fraction of ovine CMP is composed of N-acetylgalactosamine, galactose and N-glycolylneuraminic acid, molecular masses consistent with the presence of CMP containing tetra-, tri-, di- and monosaccharide were identified. |
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Palavras-Chave: |
CMP; Milk protein; Neuraminidase; Ovine casein macropeptide. |
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Thesaurus Nal: |
Acid phosphatase; Casein; Cattle; Glycosylation; Mass spectrometry; Peptides; Sheep. |
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Categoria do assunto: |
L Ciência Animal e Produtos de Origem Animal |
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Marc: |
LEADER 01743naa a2200289 a 4500
001 2090563
005 2024-01-29
008 2000 bl uuuu u00u1 u #d
100 1 $aJAVIER MORENO, F.
245 $aChromatographic characterization of ovine kappa-casein macropeptide.$h[electronic resource]
260 $c2000
520 $aAbstract: Ovine casein macropeptide (CMP) was characterized by anion-exchange FPLC and reversed-phase (RP) HPLC. To study heterogeneity (the degree of glycosylation and phosphorylation), CMP was desialylated with neuraminidase and dephosphorylated with acid phosphatase. Following RP-HPLC, the main CMP components were identified using either on-line or off-line mass spectrometry. The most abundant ovine CMP component was a diphosphorylated carbohydrate-free form, followed by one or two monophosphorylated and a non-phosphorylated asialo-aglyco species. Aglyco non-phosphorylated, monophosphorylated and diphosphorylated forms were in the ratio 3[ratio ]20[ratio ]77. Only ? 30% of ovine CMP was glycosylated. Assuming that the monosaccharide fraction of ovine CMP is composed of N-acetylgalactosamine, galactose and N-glycolylneuraminic acid, molecular masses consistent with the presence of CMP containing tetra-, tri-, di- and monosaccharide were identified.
650 $aAcid phosphatase
650 $aCasein
650 $aCattle
650 $aGlycosylation
650 $aMass spectrometry
650 $aPeptides
650 $aSheep
653 $aCMP
653 $aMilk protein
653 $aNeuraminidase
653 $aOvine casein macropeptide
700 1 $aRECIO, I.
700 1 $aOLANO, A.
700 1 $aLÓPEZ-FANDIÑO, R.
773 $tJournal of Dairy Research$gv. 6, n. 3, p. 349-359, Aug. 2000.
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Registro original: |
Embrapa Caprinos e Ovinos (CNPC) |
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