Coeliac active peptides from gliadin: large-scale preparation and characterization.
Larger amounts of coeliac active peptides are required for pathogenetic investigations. Therefore, a simplified preparative procedure by means of gel-permeation chromatography and reversed-phase HPLC was developed for the isolation of the peptides B3141-B3146, which are present in peptic tryptic digests of gliadin [this journal (1983) 176:85-94]. The peptides are derived from the N-terminal part of alpha-gliadins and are closely related. The amino acid sequence of B3143 is VPVPQLQPQNPSQQQPQEQVPLVQQQQFPGQQQQFPPQQPYPQPQPFPSQQPYL. B3144 has proline instead of glutamine in position 34. The previously described peptide B3142 [this journal (1984) 179:371-376] corresponds to B3144 except for the missing C-terminal leucine.
Wieser
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Deutsche Forschungsanstalt für Lebensmittelchemie and Institut für Lebensmittelchemie der TU München, Garching, Federal Republic of Germany.
Belitz
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HD
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D005903:Gliadin / Q000737:chemistry*; D006801:Humans; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification*
D000596:Amino Acids; D010446:Peptide Fragments; D005903:Gliadin