EDITORIAL SYNOPSIS The toxic action of wheat gluten on two patients was eliminated after predigestion of gluten by crude papain. This change is thought to be due to an enzyme which liberates ammonia from gluten. It is not thought that this particular mechanism operates in the normal intestinal cell but it is envisaged that one of the peptide bonds of the coeliac active constituent (possibly a N-glutaminyl peptide) is normally split by a specific intestinal peptidase which is defective in coeliac patients.Previous authors have shown that the harmful action of dietary wheat gluten in coeliac disease or non-tropical sprue is not eliminated by predigesting the gluten with either pancreatin or pepsin or trypsin
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