+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Isolation of celiac active peptide fractions from gliadin

Isolation of celiac active peptide fractions from gliadin

Zeitschrift fuer Lebensmittel-Untersuchung und -Forschung 176(2): 85-94

For the isolation of celiac active peptide fractions the peptic tryptic digest of whole gliadin was successively separated by ultrafiltration, gel filtration, cation-exchange chromatography, anion exchange chromatography and high-performance liquid chromatography. After each separation step the peptide fractions obtained were characterized by amino acid analysis and examined for celiac activity in an immunological test (LIF [leukocyte migration inhibition factor] test) and in an organ-culture test. The most active fractions have MW ranging from 7000-14,000 daltons, high contents of Glx (> 40 mol-%), Pro (> 20 mol-%) and Phe (> 5 mol-%) and low contents of S-containing and basic amino acids (0 and < 2.0 mol-%, respectively). The peptide fraction B3142 obtained after 5 separation steps seems to be a pure peptide, which shows activity in the immunological test for all celiac patients examined in very low concentrations. This peptide consists of 53 amino acid residues and has the composition Glx24, Pro15, Val4, Phe3, Ser2, Leu2, Asx1, Gly1, Tyr1.

Please choose payment method:

(PDF emailed within 1 workday: $29.90)

Accession: 005769510

Download citation: RISBibTeXText

PMID: 6405556

Related references

Amino acid sequence of the celiac active gliadin peptide b 3142. Zeitschrift fuer Lebensmittel-Untersuchung und -Forschung 179(5): 371-376, 1984

Immuno fluorescent serum gliadin antibodies in children with celiac disease and various mal absorptive disorders part 2 specificity of gliadin antibodies immuno globulin classes immunogenic properties of wheat protein fractions and pathogenic significance of food antibodies in celiac disease. European Journal of Pediatrics 130(3): 165-172, 1979

Isolation and enzymatic fragmentation of the coeliac-active gliadin peptide CT-1. Zeitschrift für Lebensmittel-Untersuchung und -Forschung 195(1): 22-26, 1992

Activation of macrophages by gliadin fragments: isolation and characterization of active peptide. Journal of Leukocyte Biology 71(4): 625-631, 2002

Food proteins and maturation of small intestinal microvillus membranes (MVM). II. Binding of gliadin hydrolysate fractions and of the gliadin peptide B3142. Journal of Pediatric Gastroenterology and Nutrition 7(1): 122-127, 1988

Adherence of gliadin fractions to lymphocytes in celiac disease. Lancet 1(8286): 1384-1386, 1982

Celiac anti-tissue transglutaminase antibodies interfere with the uptake of alpha gliadin peptide 31-43 but not of peptide 57-68 by epithelial cells. Biochimica et Biophysica Acta 1802(9): 717-727, 2010

Skin tests for celiac disease employing fractions of a gliadin digest. Australian Journal of Experimental Biology & Medical Science 60(4): 345-350, 1982

Testing for IgG class antibodies in celiac disease patients with selective IgA deficiency. A comparison of the diagnostic accuracy of 9 IgG anti-tissue transglutaminase, 1 IgG anti-gliadin and 1 IgG anti-deaminated gliadin peptide antibody assays. Clinica Chimica Acta; International Journal of Clinical Chemistry 382(1-2): 95-99, 2007

Amino acid composition of gliadin fractions which may be toxic to individuals with celiac disease. Clinica Chimica Acta 123(3): 311-320, 1982