Coeliac activity of the gliadin peptides CT-1 and CT-2

Z Lebensm Unters Forsch. 1986 Feb;182(2):115-7. doi: 10.1007/BF01454241.

Abstract

The coeliac active peptide B 3142, which has been isolated from a peptic-tryptic digest of gliadin and which consists of 53 amino-acid sequences, was partially hydrolyzed with alpha-chymotrypsin. The two fragment peptides CT-1 (positions 1-22 of B 3142) and CT-2 (positions 23-53) were separated by high-performance liquid chromatography on octadecyl silica gel and purified by gel filtration on Biogel P2. The examination in the organ-culture test including 18 coeliac patients on normal diet and 7 control persons have shown that the toxicity is preserved after the chymotryptic treatment and that the peptides B 3142, CT-1 and CT-2 do not significantly differ from one another according to their coeliac-specific effect.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Celiac Disease / metabolism*
  • Chromatography, Gel
  • Chromatography, High Pressure Liquid
  • Chymotrypsin
  • Gliadin / isolation & purification*
  • Gliadin / pharmacology
  • Humans
  • Hydrolysis
  • Organ Culture Techniques
  • Peptide Fragments / isolation & purification*
  • Peptide Fragments / pharmacology
  • Peptides / isolation & purification*
  • Peptides / pharmacology
  • Plant Proteins / isolation & purification*

Substances

  • Peptide Fragments
  • Peptides
  • Plant Proteins
  • gliadin peptide CT-1
  • gliadin peptide CT-2
  • gliadin peptide B 3142
  • Gliadin
  • Chymotrypsin