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The main peptides produced by hydrolysis of water buffalo β-casein with plasmin were characterized by capillary electrophoresis and mass spectrometry and compared with their bovine homologous. A novel breakdown product arising from the hydrolysis of water buffalo β-casein, originated by the presence of a plasmin-sensitive Lys bond at position 68 was identified, which was not present in bovine β-casein...
The primary structure of water buffalo αs1-casein and of β-casein A and B variants has been determined using a combination of mass spectrometry and Edman degradation procedures. The phosphorylated residues were localized on the tryptic phosphopeptides after performing a β-elimination/thiol derivatization. Water buffalo αs1-casein, resolved in three discrete bands by isoelectric focusing, was found...
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