» Articles » PMID: 1519388

Coeliac Active Peptides from Gliadin: Large-scale Preparation and Characterization

Overview
Date 1992 Mar 1
PMID 1519388
Citations 2
Authors
Affiliations
Soon will be listed here.
Abstract

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.

Citing Articles

In vitro differentiation of human monocytes into dendritic cells by peptic-tryptic digest of gliadin is independent of genetic predisposition and the presence of celiac disease.

Rakhimova M, Esslinger B, Schulze-Krebs A, Hahn E, Schuppan D, Dieterich W J Clin Immunol. 2008; 29(1):29-37.

PMID: 18696220 DOI: 10.1007/s10875-008-9228-x.


Crypt-villus differentiation reflected by lectin and protein binding to rat small intestinal brush border membranes.

Stern M, Knauss M, Stallmach A Dig Dis Sci. 1995; 40(11):2438-45.

PMID: 7587828 DOI: 10.1007/BF02063251.