Post-translational phosphorylation affects the IgE binding capacity of caseins |
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Authors: | Bernard H Meisel H Creminon C Wal J M |
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Institution: | Laboratoire d'Immuno-Allergie Alimentaire, INRA-CEA, SPI, Batiment 136, Saclay, 91191, Gif sur Yvette, France. bernardh@dsvidf2.cea.fr |
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Abstract: | IgE response specific to those molecular regions of casein that contain a major phosphorylation site was analyzed using native and modified caseins and derived peptides. This study included (i) the naturally occurring common variants A1 and A from beta- and alphas2-caseins, respectively, which were purified in the native form and then dephosphorylated, (ii) a purified rare variant D of alphas2-casein which lacks one major phosphorylation site, and (iii) the native and dephosphorylated tryptic fragment f(1-25) from beta-casein. Direct and indirect ELISA using sera from patients allergic to milk showed that the IgE response to caseins is affected by modifying or eliminating the major phosphorylation site. |
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