title: Susceptibility to denaturation of caseins in milk samples for improving protein conformational study and their identification.
abstract: Caseins are phosphoproteins kept together by non-covalent interactions to form a highly stabilised dispersion in milk. This study intended to evaluate the different effects of denaturing solvents and solutions on caseins in order to optimise the chromatographic resolution for a better identification of individual casein fractions. The caseins were obtained from bovine skimmed milks by precipitation at pH 4.3, and the proteins were dissolved in water and three different solutions. The casein separation was performed by reversed-phase high-performance liquid chromatography. Each casein was identified by matrix-assisted laser desorption ionisation-time-of-flight mass spectrometry. The best result was achieved by treating the caseins with solution D.
authors.affiliation: a Department of Pharmaceutical and Biomedical Sciences , University of Salerno , Salerno , Italy.
authors.forename: Giacomo
authors.initials: G
authors.lastname: Pepe
authors.forename: Gian Carlo
authors.initials: GC
authors.lastname: Tenore
authors.forename: Carmine
authors.initials: C
authors.lastname: Conte
authors.forename: Mariateresa
authors.initials: M
authors.lastname: Russo
authors.forename: Michele
authors.initials: M
authors.lastname: Manfra
authors.forename: Pietro
authors.initials: P
authors.lastname: Campiglia
mesh_terms: D000818:Animals; D002364:Caseins / Q000737:chemistry*; D002417:Cattle; D013058:Mass Spectrometry; D008892:Milk / Q000737:chemistry*; D011489:Protein Denaturation
chemical_list: D002364:Caseins