Coeliac disease: the abolition of gliadin toxicity by enzymes from Aspergillus niger.
1. Gliadin from which carbohydrate was removed by treatment with carbohydrase from Aspergillus niger was fed to three coeliac patients in remission. 2. Xylose absorption, mucosal morphology and brush-border enzymes were used to assess the toxicity of the carbohydrase-treated gliadin. 3. Gliadin treated with carbohydrases did not damage the intestinal mucosa of the coeliac patients. 4. The primary structure of the gliadin proteins was not altered by the enzyme treatment.
D000293:Adolescent; D000328:Adult; D001234:Aspergillus niger / Q000201:enzymology; D002446:Celiac Disease / Q000378:metabolism* / Q000473:pathology; D005260:Female; D005903:Gliadin / Q000009:adverse effects / Q000378:metabolism*; D006801:Humans; D007408:Intestinal Absorption; D007583:Jejunum / Q000473:pathology; D008297:Male; D008875:Middle Aged; D010455:Peptides / Q000032:analysis; D010940:Plant Proteins / Q000378:metabolism*; D014994:Xylose / Q000378:metabolism
D010455:Peptides; D010940:Plant Proteins; D005903:Gliadin; D014994:Xylose