Isolation and enzymatic fragmentation of the coeliac-active gliadin peptide CT-1.
Investigations on the structure/toxicity relationships of gliadin peptides were continued with the coeliac-active gliadin peptide CT-1, which is derived from the N-terminal portion (residues 3-24 of the amino acid sequence) of alpha-gliadins [this journal (1986) 182:115-117]. CT-1 was produced by chymotryptic digestion and reversed-phase (RP) HPLC from the peptide fraction G3 [this journal (1992) 194:1-6] and digested with the proteases endoproteinase Glu-C, pancreatin, papain and thermolysin. The fragment peptides were separated by preparative RP-HPLC and characterized by amino acid analysis. On the basis of the specificity of the enzymes for CT-1 and the toxic effect of enzymatic hydrolysates of gliadin described in the literature, the significance of partial sequences, in particular of the sequence -Pro-Ser-Gln-Gln-Gln-Pro- for the coeliac-toxicity effect, is discussed.
Wieser
H
H
Deutsche Forschungsanstalt für Lebensmittelchemie, Technical University Munich, Garching, Federal Republic of Germany.
Belitz
H D
HD
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D002918:Chymotrypsin / Q000378:metabolism; D005903:Gliadin / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D008969:Molecular Sequence Data; D010194:Pancreatin / Q000378:metabolism; D010206:Papain / Q000378:metabolism; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D012697:Serine Endopeptidases / Q000378:metabolism; D013379:Substrate Specificity; D013820:Thermolysin / Q000378:metabolism
D010446:Peptide Fragments; C048574:gliadin peptide CT-1; D010194:Pancreatin; D005903:Gliadin; D012697:Serine Endopeptidases; D002918:Chymotrypsin; C028344:glutamyl endopeptidase; D010206:Papain; D013820:Thermolysin