The aim of this work was to check and quantify any cross-reactivities among the main bovine whey proteins, utilizing purified polyclonal antibodies against bovine ?-lactoglobulin, ?-lactalbumin and serum albumin, and to identify possible common epitope(s). Purified polyclonal anti-bovine ?-lactoglobulin antibodies show 10% cross-reactivity with bovine ?-lactalbumin, both in its native and its denaturated form. A continous stretch of four amino acids common to ?-lactalbumin and ?-lactoglobulin that might be responsible for this cross-reactivity has been identified. Cross-reactivity between this antibody and bovine serum albumin is, on the contrary, negligible. Purified polyclonal anti-bovine ?-lactalbumin and anti-serum albumin antibodies do not cross-react.
Evidence for a common epitope between bovine alpha-lactalbumin and beta-lactoglobulin
Giuffrida;M G;Napolitano L;Conti;
1998
Abstract
The aim of this work was to check and quantify any cross-reactivities among the main bovine whey proteins, utilizing purified polyclonal antibodies against bovine ?-lactoglobulin, ?-lactalbumin and serum albumin, and to identify possible common epitope(s). Purified polyclonal anti-bovine ?-lactoglobulin antibodies show 10% cross-reactivity with bovine ?-lactalbumin, both in its native and its denaturated form. A continous stretch of four amino acids common to ?-lactalbumin and ?-lactoglobulin that might be responsible for this cross-reactivity has been identified. Cross-reactivity between this antibody and bovine serum albumin is, on the contrary, negligible. Purified polyclonal anti-bovine ?-lactalbumin and anti-serum albumin antibodies do not cross-react.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
