At present, compared with bovine milk, the characterization of donkey milk caseins is at a relatively early stage progress, and only limited data are related to its genetic polymorphism. In this work, the heterogeneity of donkey caseome was investigated using a proteomic approach, based on one- (PAGE, UTLIEF) and two-dimensional (PAGE→UTLIEF) electrophoresis, stained with either Coomassie Brilliant Blue or specific polyclonal antibodies, and structuralMSanalysis. These combined methodologies allowed the contemporary identification of donkey as1, as2, b and k-CN with their related heterogeneity due to phosphorylation (as1,as2 and b-CN), glycosylation (k-CN) and incorrect splicing of RNA in mRNA (deleted forms of as1-CN and b-CN). The results achieved showed 11 components for k-CN, six phosphorylated components for b and as1-CN and three main phosphorylated components for as2-CN, each accounting for 10, 11 and 12 P/mole. At this regard, for the first time, the primary structure of the expressed protein corresponding to the only available donkey as2-CN cDNA sequence was determined. Furthermore b-CN was found in homozygous and heterozygous state for the occurrence of a genetic b-CN variant having a MW value 28 mass units higher than the common b-CN phenotype.
Proteomic characterization of donkey milk “caseome" / Chianese, Lina; Calabrese, M. G.; Ferranti, Pasquale; Mauriello, Rosalba; Garro, Giuseppina; DE SIMONE, C.; Quarto, Maria; Addeo, Francesco; Cosenza, Gianfranco; Ramunno, Luigi. - In: JOURNAL OF CHROMATOGRAPHY A. - ISSN 0021-9673. - ELETTRONICO. - 1217:(2010), pp. 4834-4840. [10.1016/j.chroma.2010.05.017]
Proteomic characterization of donkey milk “caseome"
CHIANESE, LINA;FERRANTI, PASQUALE;MAURIELLO, ROSALBA;GARRO, GIUSEPPINA;QUARTO, MARIA;ADDEO, FRANCESCO;COSENZA, GIANFRANCO;RAMUNNO, LUIGI
2010
Abstract
At present, compared with bovine milk, the characterization of donkey milk caseins is at a relatively early stage progress, and only limited data are related to its genetic polymorphism. In this work, the heterogeneity of donkey caseome was investigated using a proteomic approach, based on one- (PAGE, UTLIEF) and two-dimensional (PAGE→UTLIEF) electrophoresis, stained with either Coomassie Brilliant Blue or specific polyclonal antibodies, and structuralMSanalysis. These combined methodologies allowed the contemporary identification of donkey as1, as2, b and k-CN with their related heterogeneity due to phosphorylation (as1,as2 and b-CN), glycosylation (k-CN) and incorrect splicing of RNA in mRNA (deleted forms of as1-CN and b-CN). The results achieved showed 11 components for k-CN, six phosphorylated components for b and as1-CN and three main phosphorylated components for as2-CN, each accounting for 10, 11 and 12 P/mole. At this regard, for the first time, the primary structure of the expressed protein corresponding to the only available donkey as2-CN cDNA sequence was determined. Furthermore b-CN was found in homozygous and heterozygous state for the occurrence of a genetic b-CN variant having a MW value 28 mass units higher than the common b-CN phenotype.File | Dimensione | Formato | |
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