Proteomic characterization of donkey milk 'caseome'

UTLIEF) electrophoresis, stained with either Coomassie Brilliant Blue or specific polyclonal antibodies, and structural MS analysis. These combined methodologies allowed the contemporary identification of donkey alpha(s1), alpha(s2), beta and kappa-CN with their related heterogeneity due to phosphorylation (alpha(s1), alpha(s2) and beta-CN), glycosylation (kappa-CN) and incorrect splicing of RNA in mRNA (deleted forms of alpha(s1)-CN and beta-CN). The results achieved showed 11 components for kappa-CN, six phosphorylated components for beta and alpha(s1)-CN and three main phosphorylated components for alpha(s2)-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 alpha(s2)-CN cDNA sequence was determined. Furthermore beta-CN was found in homozygous and heterozygous state for the occurrence of a genetic beta-CN variant having a MW value 28 mass units higher than the common beta-CN phenotype. -->
Popis souboru: ELETTRONICO
Jazyk: English
Přístupová URL adresa: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be54a7b5c1e56d672107ad5cd18f5c61
http://hdl.handle.net/11588/371424
Rights: CLOSED
Přírůstkové číslo: edsair.doi.dedup.....be54a7b5c1e56d672107ad5cd18f5c61
Autor: Pasquale Ferranti, Carmela De Simone, Maria Grazia Calabrese, Maria Quarto, Giuseppina Garro, Lina Chianese, Francesco Addeo, Luigi Ramunno, Gianfranco Cosenza, Rosalba Mauriello
Přispěvatelé: Chianese, Lina, Calabrese, M. G., Ferranti, Pasquale, Mauriello, Rosalba, Garro, Giuseppina, DE SIMONE, C., Quarto, Maria, Addeo, Francesco, Cosenza, Gianfranco, Ramunno, Luigi
Jazyk: angličtina
Rok vydání: 2010
Předmět:
Popis: 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 structural MS analysis. These combined methodologies allowed the contemporary identification of donkey alpha(s1), alpha(s2), beta and kappa-CN with their related heterogeneity due to phosphorylation (alpha(s1), alpha(s2) and beta-CN), glycosylation (kappa-CN) and incorrect splicing of RNA in mRNA (deleted forms of alpha(s1)-CN and beta-CN). The results achieved showed 11 components for kappa-CN, six phosphorylated components for beta and alpha(s1)-CN and three main phosphorylated components for alpha(s2)-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 alpha(s2)-CN cDNA sequence was determined. Furthermore beta-CN was found in homozygous and heterozygous state for the occurrence of a genetic beta-CN variant having a MW value 28 mass units higher than the common beta-CN phenotype.
Databáze: OpenAIRE