MEASUREMENT OF GLUTEN USING A MONOCLONAL-ANTIBODY TO A SEQUENCED PEPTIDE OF ALPHA-GLIADIN FROM THE CELIAC-ACTIVATING DOMAIN-I

被引：23
作者：
ELLIS, HJ
DOYLE, AP
WIESER, H
STURGESS, RP
DAY, P
CICLITIRA, PJ
机构：
[1] ST THOMAS HOSP,RAYNE INST,LONDON SE1 7EH,ENGLAND
[2] GERMAN RES INST FOOD CHEM,D-80466 GARCHING,GERMANY
来源：
JOURNAL OF BIOCHEMICAL AND BIOPHYSICAL METHODS | 1994年 / 28卷 / 01期
关键词：
GLUTEN; GLIADIN; PROLAMIN; CELIAC DISEASE;
D O I：
10.1016/0165-022X(94)90066-3
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
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页码：77 / 82
页数：6
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