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Post‐translational phosphorylation affects the IgE binding capacity of caseins
Author(s) -
Bernard H.,
Meisel H.,
Cremi C.,
Wal J.M.
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01164-9
Subject(s) - phosphorylation , casein , chemistry , immunoglobulin e , biochemistry , microbiology and biotechnology , biology , antibody , immunology
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 β‐ and αs2‐caseins, respectively, which were purified in the native form and then dephosphorylated, (ii) a purified rare variant D of αs2‐casein which lacks one major phosphorylation site, and (iii) the native and dephosphorylated tryptic fragment f(1–25) from β‐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.