Detection and identification of a soy protein component that cross react with caseins from cow milk

ROZENFELD PA; DOCENA GH; ANON MC; FOSSATI CA

CLINICAL AND EXPERIMENTAL IMMUNOLOGY

Año: 2002 vol. 130 p. 49 - 58

0009-9104

Soy-based formulas are the most employed cow’s milk substitutes in the treatment of cow’s milk allergy in our country. Since adverse reactions have been reported in allergic patients as a consequence of exposure to soy proteins, we have investigated the possible cross-reactivity between components from soybean and cow’s milk. A cow’s milk specific polyclonal antiserum and casein specific monoclonal antibodies were used in immunoblotting and competitive ELISA studies to identify a 30-kD component from soybean that cross-reacts with cow’s milk caseins. Its IgE binding capacity was tested by EAST, employing sera from cow’s milk allergic patients, not previously exposed to soy proteins. The 30kD protein was isolated and partially sequenced. It is constituted by two polypeptides (A5 and B3) linked by a disulphide bond. The protein’s capacity to bind to the different antibodies relies on the B3 by a disulphide bond. The protein’s capacity to bind to the different antibodies relies on the B3 by a disulphide bond. The protein’s capacity to bind to the different antibodies relies on the B3 by a disulphide bond. The protein’s capacity to bind to the different antibodies relies on the B3 by a disulphide bond. The protein’s capacity to bind to the different antibodies relies on the B3 by a disulphide bond. The protein’s capacity to bind to the different antibodies relies on the B3 by a disulphide bond. The protein’s capacity to bind to the different antibodies relies on the B3 5 and B3) linked by a disulphide bond. The protein’s capacity to bind to the different antibodies relies on the B33 poly-peptide. These results indicate that soy-based formula, which contains the A5-B3 glycinin molecule, could be involved in allergic reactions observed in cow’s milk allergic patients exposed to soy-containing foods.