Post-translational phosphorylation affects the IgE binding capacity of caseins

被引:57
作者
Bernard, H
Meisel, H
Creminon, C
Wal, JM
机构
[1] CEA, INRA, SPI, Lab Immunoallergie Alimentaire, F-91191 Gif Sur Yvette, France
[2] CEA Saclay, Serv Pharmacol & Immunol, F-91191 Gif Sur Yvette, France
[3] Bundesanstalt Milchforsch, Inst Chem & Phys, D-2300 Kiel, Germany
关键词
allergy; IgE; casein; phosphorylation site;
D O I
10.1016/S0014-5793(00)01164-9
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
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 beta- and alpha s2-caseins, respectively, which were purified in the native form and then dephosphorylated, (ii) a purified rare variant D of alpha s2-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. (C) 2000 Federation of European Biochemical Societies.
引用
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页码:239 / 244
页数:6
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