Abstract
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Highlights
Cow milk casein consists of several fractions each of which have different structure and differing antigenicity
The aim of the study was to investigate the capacity of cow milk casein, casein fractions, casein hydrolysate and its fractions to bind human IgG antibodies
The antigenicity of the casein hydrolysate compared to nonhydrolysed casein was reduced down to 18.5 and 41.8% measured with patient and control sera, respectively
Summary
Cow milk casein consists of several fractions each of which have different structure and differing antigenicity. The aim of the study was to investigate the capacity of cow milk casein, casein fractions, casein hydrolysate and its fractions to bind human IgG antibodies (antigenicity). Identification of cow milk caseins and its fractions with the highest bindnig capacity for human IgG antibodies is important for manufacturing of antigen-reduced formulas based on casein hydrolysates. Antigenic reactivity of a protein refers to its capacity to bind to the functional binding sites or paratopes of certain immunoglobulin molecules (van Regenmortel 1988). This is different among proteins due to the manifold quality and quantity of their specific epitopes.
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