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Specific IgE responses in patients allergic to goat’s milk but tolerant to cow’s milk: involvement of minor differences in primary structure between caprine and bovine caseins
Author(s) -
AhLeung Sandrine,
Blanc Fany,
Hazebrouck Stéphane,
AdelPatient Karine,
Paty Evelyne,
Scheinmann Pierre,
Wal JeanMichel,
Bernard Hervé
Publication year - 2011
Publication title -
clinical and translational allergy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.979
H-Index - 37
ISSN - 2045-7022
DOI - 10.1186/2045-7022-1-s1-o9
Subject(s) - medicine , bovine milk , immunoglobulin e , cow's milk allergy , allergy , immunology , milk allergy , food science , food allergy , antibody , biology
Methods b-Lactoglobulin, whole casein and its four different fractions, i.e. as1-, as2-, band -caseins, were isolated from raw CM and GM. Purified b-caseins were subjected to a mild proteolysis by plasmin which generated 3 peptides, i.e. f(1-28), f(29-107) and f(108-207/9). Synthetic peptides partially recovering the N-terminal f(29107) part of the caprine b-casein were also produced. Immunoreactivity of the purified proteins and peptides was assessed by IgE binding studies using sera from 12 GM-allergic patients tolerant to CM and 10 CM-allergic patients. The capacity of bovine and caprine milk proteins to induce the degranulation of humanized rat mast cells passively sensitized with human specific IgE was also evaluated.

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