Measurement of gluten using a monoclonal antibody to a sequenced peptide of alpha-gliadin from the coeliac-activating domain I.
A monoclonal antibody, raised against a sequenced 54 amino-acid peptide from the coeliac-activating N-terminal region of alpha-gliadin, was used in an assay for the measurement of gluten in foods. A double-sandwich ELISA using a polyclonal capture antibody produced standard curves for unfractionated gliadin and its alpha, beta, gamma and omega subfractions, and for rye, barley and oat prolamins. The sensitivity of the assay for unfractionated gliadin and rye prolamins was 15 ng/ml, for barley and oat prolamins 125 and 250 ng/ml, respectively. Prolamins from coeliac non-toxic rice, maize, millet and sorghum did not cross-react in the assay.
Ellis
H J
HJ
Rayne Institute, St. Thomas' Hospital, London, UK.
Doyle
A P
AP
Wieser
H
H
Sturgess
R P
RP
Day
P
P
Ciclitira
P J
PJ
D000911:Antibodies, Monoclonal; D002446:Celiac Disease / Q000378:metabolism; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes / Q000276:immunology; D005903:Gliadin / Q000032:analysis / Q000276:immunology*; D005983:Glutens / Q000032:analysis*; D010446:Peptide Fragments / Q000276:immunology; D010940:Plant Proteins / Q000032:analysis*; D012680:Sensitivity and Specificity
D000911:Antibodies, Monoclonal; D000939:Epitopes; D010446:Peptide Fragments; D010940:Plant Proteins; D005983:Glutens; D005903:Gliadin