Digested Ara h 1 Loses Sensitizing Capacity When Separated into Fractions
Publication: Research - peer-review › Journal article – Annual report year: 2012
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Digested Ara h 1 Loses Sensitizing Capacity When Separated into Fractions. / Bøgh, Katrine Lindholm; Barkholt, Vibeke; Rigby, Neil M.; Mills, E. N. Clare; Madsen, Charlotte Bernhard.
In: Journal of Agricultural and Food Chemistry, Vol. 60, No. 11, 2012, p. 2934-2942.Publication: Research - peer-review › Journal article – Annual report year: 2012
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TY - JOUR
T1 - Digested Ara h 1 Loses Sensitizing Capacity When Separated into Fractions
A1 - Bøgh,Katrine Lindholm
A1 - Barkholt,Vibeke
A1 - Rigby,Neil M.
A1 - Mills,E. N. Clare
A1 - Madsen,Charlotte Bernhard
AU - Bøgh,Katrine Lindholm
AU - Barkholt,Vibeke
AU - Rigby,Neil M.
AU - Mills,E. N. Clare
AU - Madsen,Charlotte Bernhard
PB - American Chemical Society
PY - 2012
Y1 - 2012
N2 - The major peanut allergen Ara h 1 is an easily digestible protein under physiological conditions. The present study revealed that pepsin digestion products of Ara h 1 retained the sensitizing potential in a Brown Norway rat model, while this sensitizing capacity was lost by separating the digest into fractions by gel permeation chromatography. Protein chemical analysis showed that the peptide composition as well as the aggregation profiles of the fractions of Ara h 1 digest differed from that of the whole pool. These results indicate that the sensitizing capacity of digested Ara h 1 is a consequence of the peptides being in an aggregated state resembling the intact molecule or that most peptides of the digests need to be present in the same solution, having a synergistic or adjuvant effect and thereby augmenting the immune response against other peptides.
AB - The major peanut allergen Ara h 1 is an easily digestible protein under physiological conditions. The present study revealed that pepsin digestion products of Ara h 1 retained the sensitizing potential in a Brown Norway rat model, while this sensitizing capacity was lost by separating the digest into fractions by gel permeation chromatography. Protein chemical analysis showed that the peptide composition as well as the aggregation profiles of the fractions of Ara h 1 digest differed from that of the whole pool. These results indicate that the sensitizing capacity of digested Ara h 1 is a consequence of the peptides being in an aggregated state resembling the intact molecule or that most peptides of the digests need to be present in the same solution, having a synergistic or adjuvant effect and thereby augmenting the immune response against other peptides.
KW - AGRICULTURE,
KW - CHEMISTRY,
KW - FOOD
KW - MAJOR PEANUT ALLERGEN
KW - B-CELL EPITOPES
KW - STRUCTURE-IMMUNOGENICITY RELATIONSHIP
KW - IGE-BINDING EPITOPES
KW - FOOD ALLERGENS
KW - SYNTHETIC PEPTIDES
KW - IN-VITRO
KW - GASTROINTESTINAL DIGESTION
KW - MILK-PROTEINS
KW - ANTIBODIES
U2 - 10.1021/jf2052306
DO - 10.1021/jf2052306
JO - Journal of Agricultural and Food Chemistry
JF - Journal of Agricultural and Food Chemistry
SN - 0021-8561
IS - 11
VL - 60
SP - 2934
EP - 2942
ER -