FEBS Letters | |
Post‐translational phosphorylation affects the IgE binding capacity of caseins | |
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
【 预 览 】
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