Title page for ETD etd-06082009-170848


Type of Document Master's Thesis
Author Jasti, Sunitha
URN etd-06082009-170848
Title Separation of gliadin peptides for investigation of the injurious agent(s) in gluten sensitive enteropathy
Degree Master of Science
Department Human Nutrition and Foods
Advisory Committee
Advisor Name Title
Barbeau, William E. Committee Chair
Bevan, David R. Committee Member
Novascone, Mary Ann Committee Member
Keywords
  • peptides
  • wheat
Date of Defense 1995-01-12
Availability restricted
Abstract

Crude gliadins isolated from three wheat varieties (Karl, Tam 107 and CS- 93) were subjected to in vitro hydrolysis by the extracellular enzymes pepsin, peptidase and pancreatin. Gliadins from one variety (Karl) also were exposed to the intracellular enzymes cathepsins Band D. A reverse phase high performance liquid chromatography (RP-HPLC) method was developed to separate unhydrolyzed and hydrolyzed gliadins. The unhydrolyzed crude gliadins were resolved into 12-14 peaks, with at least five peaks that appeared to be common to all three wheat varieties. Gliadin peptides were resolved into between 44 and 71 peaks, suggesting that a large numbers of peptides are derived from proteins present in more than one of the four major gliadin fractions (i.e.; α, β, γ, and ω - gliadins). No major differences were detected between chromatograms of extracellular digests and those of extracellular /intracellular digests indicating that cathepsins Band D may not contribute to more complete gliadin digestion. The molecular weights and amino acid sequences of gliadin peptides will need to be determined by HPLC mass spectrometry (HPLC-MS) for accurate qualitative and/or quantitative comparisons of individual digests. Our in vitro hydrolysis/RP-HPLC methods may be applicable, however, in the generation of celiac active peptides for future toxicity testing.

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