Post‐translational phosphorylation affects the IgE binding capacity of caseins

FEBS Letters

Creminon, C.²  Wal, J.M.³  Bernard, H.³  Meisel, H.¹ 

[1] Institut für Chemie und Physik, Bundesanstalt für Milchforschung, Kiel, Germany;CEA, Service de Pharmacologie et d'Immunologie, CEA-Saclay, 91191 Gif sur Yvette, France;Laboratoire d'Immuno-Allergie Alimentaire, INRA-CEA, SPI, Bâtiment 136, Saclay, 91191 Gif sur Yvette, France

关键词: Allergy;    IgE;    Casein;    Phosphorylation site;    Ig;    immunoglobulin;    ELISA;    enzyme-linked immunosorbent assay;    EIA;    enzyme immunoassay;    E/S;    enzyme/substrate ratio;    RP-HPLC;    reversed phase high performance liquid chromatography;    TFA;    trifluoroacetic acid;    HSA;    human serum albumin;    EDTA;    ethylenediaminetetraacetic acid;    FPLC;    fast protein liquid chromatography;   

DOI  :  10.1016/S0014-5793(00)01164-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown