Isolation and analysis of peptidic fragments of α-gliadin using reversed-phase high-performance liquid chromatography

Kocna, Petr; Frič, P; Kočová-Holáková, Marie; Slabý, J; Kasafírek, E; Hekkens, W. Th. J. M.

doi:10.1016/s0378-4347(88)80010-0

Cited by 5 publications

References 21 publications

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Relationship between gliadin peptide structure and their effect on the fetal chick duodenum

Kocna

Mothes

Krchňák

et al. 1991

Z Lebensm Unters Forch

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The tendency to form a beta-turn in alpha-gliadin was estimated using the B-cell determinant prediction program based on the Chou and Fasman probability of beta-turn formation. Six sequences possessing a high probability of beta-turn formation were found. A statistically high agreement was found between these six sequences and three areas in alpha-gliadin with the occurrence of Pro-Ser-Gln-Gln sequence which has recently been considered responsible for toxicity in coeliac disease. By means of solid-phase synthesis seven peptides were obtained covering the above-mentioned regions. Their toxicity was tested using the fetal chick duodenum. The results support the suggestion that peptides containing the sequences Pro-Ser-Gln-Gln and Gln-Gln-Gln-Pro may be involved in the pathogenesis of coeliac disease.

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Relationship between gliadin peptide structure and their effect on the fetal chick duodenum

Kocna

Mothes

Krchňák

et al. 1991

Z Lebensm Unters Forch

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Characterization of human, mouse and rabbit anti-gliadin antibodies by ELISA and western blotting

et al. 1995

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Monoclonal, hyperimmune rabbit and human serum anti-gliadin antibodies were analyzed by ELISA and immunoblotting techniques. In Western blotting the difference in reactivity between monoclonal and human antibodies was quantitative rather than qualitative. Rabbit antisera differed in reactivity according to the protein used for immunization. The rabbits immunized by the peptic-tryptic pancreatic digest of gliadin reacted similarly to the patients. In ELISA, significantly higher reactivity with crude, A-, glyc-gli, alpha-, beta- and omega-gliadins was found in the patients' sera than in controls.

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Gluten Metabolism in Humans

Caminero

Nistal

Herrán

et al. 2014

Wheat and Rice in Disease Prevention and Health

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Isolation and analysis of peptidic fragments of α-gliadin using reversed-phase high-performance liquid chromatography

Cited by 5 publications

References 21 publications

Relationship between gliadin peptide structure and their effect on the fetal chick duodenum

Relationship between gliadin peptide structure and their effect on the fetal chick duodenum

Characterization of human, mouse and rabbit anti-gliadin antibodies by ELISA and western blotting

Gluten Metabolism in Humans

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