{"id":{"repo_id":"vt","oai_identifier":"oai:vtechworks.lib.vt.edu:10919/42893"},"canonical_url":"https://search.dev.ndltd.org/etd/vt/oai:vtechworks.lib.vt.edu:10919/42893","repository":{"repo_id":"vt","name":"Virginia Tech","base_url":"https://vtechworks.lib.vt.edu/oai/request"},"display":{"title":"Separation of gliadin peptides for investigation of the injurious agent(s) in gluten sensitive enteropathy","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 Ï - 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.","abstract_html":"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 Ï - 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.","abstract_has_math":false,"creators":["Jasti, Sunitha"],"institution":"Virginia Tech","degree_name":"Master of Science","degree_level":"masters","degree_discipline":"Human Nutrition and Foods","degree_department":"Human Nutrition and Foods","school":null,"contributors":[],"advisors":[],"committee_chairs":["Barbeau, William E."],"committee_members":["Novascone, Mary Ann","Bevan, David R."],"year":1995,"date_issued":"1995-01-12","date_published":"1995-01-12","updated_at":"2026-07-22T22:19:42Z","subjects":["peptides","wheat"],"languages":["en"],"rights":["In Copyright"],"rights_urls":["http://rightsstatements.org/vocab/InC/1.0/"],"identifier_entries":[{"key":"dc:identifier.other","label":"Dc Identifier Other","values":["etd-06082009-170848"],"render_values":[{"text":"etd-06082009-170848","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/10919/42893","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.committeechair","label":"Committee Chair","values":["Barbeau, William E."]},{"key":"dc:contributor.committeemember","label":"Committee Member","values":["Novascone, Mary Ann","Bevan, David R."]},{"key":"dc:contributor.department","label":"Department","values":["Human Nutrition and Foods"]},{"key":"dc:creator","label":"Author","values":["Jasti, Sunitha"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2014-03-14T21:37:06Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2014-03-14T21:37:06Z","2009-06-08"]},{"key":"dc:date.issued","label":"Date","values":["1995-01-12"]},{"key":"dc:publisher","label":"Institution","values":["Virginia Tech"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]},{"key":"dc:type.dcmitype","label":"Dc Type Dcmitype","values":["Text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Human Nutrition and Foods"]},{"key":"thesis:degree_level","label":"Degree Level","values":["masters"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Master of Science"]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["Virginia Polytechnic Institute and State University"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["peptides","wheat"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language.iso","label":"Language (ISO)","values":["en"]},{"key":"dc:rights","label":"Dc Rights","values":["In Copyright"]},{"key":"dc:rights.uri","label":"Rights URI","values":["http://rightsstatements.org/vocab/InC/1.0/"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.other","label":"Dc Identifier Other","values":["etd-06082009-170848"]},{"key":"dc:identifier.uri","label":"Identifier URI","values":["http://hdl.handle.net/10919/42893"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["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 Ï - 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."]},{"key":"dc:description.degree","label":"Dc Description Degree","values":["Master of Science"]},{"key":"dc:format.medium","label":"Dc Format Medium","values":["BTD"]},{"key":"dc:format.mimetype","label":"Dc Format Mimetype","values":["application/pdf"]},{"key":"dc:title","label":"Title","values":["Separation of gliadin peptides for investigation of the injurious agent(s) in gluten sensitive enteropathy"]}]}],"canonical_facts":{"dc:contributor.committeechair":["Barbeau, William E."],"dc:contributor.committeemember":["Novascone, Mary Ann","Bevan, David R."],"dc:contributor.department":["Human Nutrition and Foods"],"dc:creator":["Jasti, Sunitha"],"dc:date.accessioned":["2014-03-14T21:37:06Z"],"dc:date.available":["2014-03-14T21:37:06Z","2009-06-08"],"dc:date.issued":["1995-01-12"],"dc:description.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. 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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. 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