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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.

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Accession: 005769510

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PMID: 6405556


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