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 beta-lactoglobulin, alpha-lactalbumin and serum albumin, and to identify possible common epitope(s). Purified polyclonal anti-bovine beta-lactoglobulin antibodies show 10% cross-reactivity with bovine alpha-lactalbumin, both in its native and its denatured form. A continuous stretch of four amino acids common to alpha-lactalbumin and beta-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 alpha-lactalbumin and anti-serum albumin antibodies do not cross-react.

Evidence for a common epitope between bovine alfa-lactalbumin and beta-lactoglobulin

BERTINO, Enrico;FABRIS, Claudio;
1998-01-01

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 beta-lactoglobulin, alpha-lactalbumin and serum albumin, and to identify possible common epitope(s). Purified polyclonal anti-bovine beta-lactoglobulin antibodies show 10% cross-reactivity with bovine alpha-lactalbumin, both in its native and its denatured form. A continuous stretch of four amino acids common to alpha-lactalbumin and beta-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 alpha-lactalbumin and anti-serum albumin antibodies do not cross-react.
1998
379(12)
1453
1456
Baroglio C; Giuffrida MG; Cantisani A; Napolitano L; Bertino E; Fabris C; Conti A.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2318/90408
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