Abstract
In bovine milk intolerance β-Lactoglobuline (β-Lg) is more allergenic than α-Lactalbumine (α-La) and β-casein (β-cas). We studied the two major limiting steps to the transfer of the milk protein antigens to blood, i.e. hydrolysis and epithelial permeability.
Methods: In vitro pepsin-trypsin hydrolysis was measured by disappearance of protein antigens (ELISA) and appearance of α-NH2 residua. The transepithelial fluxes for antigenic determinants (ELISA) and degraded products (isotopic measurment) were performed in Isolated stripped rabbit ileum in Ussing chamber in vitro.
Results: Pepsin-trypsin hydrolysis showed an increasing resistance In the order β-cas <α-La < β-Lg. The rate of intracellular hydrolysis was in the same order (β-Lg the most resistant to hydrolysis). The fluxes of antlgenic determinants across the epithelium was β-Lg > α-La > β-cas, i.e. 412, 135 and not detectable ng/h.cm2 respectively. These results indicate a selective intestinal mucoeal permeability for milk protein antigens. This selectivity may play a role in allergenicity.
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Marcon-Genty, D., Kheroua, O., Tomé, D. et al. Intestinal transepithelial passage of bovine milk protein antigens in vitro. Pediatr Res 22, 223 (1987). https://doi.org/10.1203/00006450-198708000-00059
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DOI: https://doi.org/10.1203/00006450-198708000-00059