Polyclonal antibodies raised against synthetic peptides reproducing sequence stretches of bovine alpha(s1)-casein were used as probes to discriminate within the alpha(s1)-casein fraction of bovine milk and cheese. A minor alpha(s1)-casein component, selectively recognized by an antisera directed against the bovine 139-149 alpha(s1)-casein sequence, was found to be a C-terminally truncated alpha(s1)-casein form. This component coeluted with the main alpha(s1)- and alpha(s2)-casein by anion-exchange chromatography of whole casein, whereas by RP-HPLC it eluted with alpha(s2)-casein only. Similarly to the main alpha(s1)-casein, the C-terminally truncated form was hydrolyzed in vitro by chymosin and early in the cheesemaking.
Antipeptide antibodies as analytical tools to discriminate among bovine alpha(s1)-casein components
Pizzano R;
1998
Abstract
Polyclonal antibodies raised against synthetic peptides reproducing sequence stretches of bovine alpha(s1)-casein were used as probes to discriminate within the alpha(s1)-casein fraction of bovine milk and cheese. A minor alpha(s1)-casein component, selectively recognized by an antisera directed against the bovine 139-149 alpha(s1)-casein sequence, was found to be a C-terminally truncated alpha(s1)-casein form. This component coeluted with the main alpha(s1)- and alpha(s2)-casein by anion-exchange chromatography of whole casein, whereas by RP-HPLC it eluted with alpha(s2)-casein only. Similarly to the main alpha(s1)-casein, the C-terminally truncated form was hydrolyzed in vitro by chymosin and early in the cheesemaking.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
