{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/72524"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/72524","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Characterization and Analysis of Anti-Metatype Antibodies","abstract":"Immunizations of high affinity anti-fluorescein monoclonal antibody 4-4-20 affinity-labeled with fluorescein 5-isothiocyanate into rabbit elicited antibodies specific for the liganded conformation of 4-4-20. Termed anti-metatype antibodies, this polyclonal reagent also demonstrated the unique ability to delay the rate of dissociation of fluorescyl ligand from the active site of 4-4-20. This delay led to an artificial enhancement of the affinity of 4-4-20 for fluorescyl ligand. Utilization of a single chain derivative of 4-4-20 confirmed that anti-metatype reactivity was variable-region specific. Additionally, anti-metatype antibodies reacted with members of the 4-4-20 idiotype family, demonstrating varying degrees of affinity enhancement with idiotypically related molecules.","abstract_html":"Immunizations of high affinity anti-fluorescein monoclonal antibody 4-4-20 affinity-labeled with fluorescein 5-isothiocyanate into rabbit elicited antibodies specific for the liganded conformation of 4-4-20. Termed anti-metatype antibodies, this polyclonal reagent also demonstrated the unique ability to delay the rate of dissociation of fluorescyl ligand from the active site of 4-4-20. This delay led to an artificial enhancement of the affinity of 4-4-20 for fluorescyl ligand. Utilization of a single chain derivative of 4-4-20 confirmed that anti-metatype reactivity was variable-region specific. Additionally, anti-metatype antibodies reacted with members of the 4-4-20 idiotype family, demonstrating varying degrees of affinity enhancement with idiotypically related molecules.","abstract_has_math":false,"creators":["Weidner, Karla Marie"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Microbiology","degree_department":null,"school":null,"contributors":["Voss, Edward W., Jr."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2014,"date_issued":"2014-12-17T23:15:37Z","date_published":"2014-12-17T23:15:37Z","updated_at":"2026-07-22T22:26:07Z","subjects":["Chemistry, Biochemistry","Health Sciences, Immunology"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(UMI)AAI9305728"],"render_values":[{"text":"(UMI)AAI9305728","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/72524","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Voss, Edward W., Jr."]},{"key":"dc:creator","label":"Author","values":["Weidner, Karla Marie"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2014-12-17T23:15:37Z","10000-01-01","1992"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Microbiology"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Illinois at Urbana-Champaign"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Chemistry, Biochemistry","Health Sciences, Immunology"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/72524","(UMI)AAI9305728"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Immunizations of high affinity anti-fluorescein monoclonal antibody 4-4-20 affinity-labeled with fluorescein 5-isothiocyanate into rabbit elicited antibodies specific for the liganded conformation of 4-4-20. Termed anti-metatype antibodies, this polyclonal reagent also demonstrated the unique ability to delay the rate of dissociation of fluorescyl ligand from the active site of 4-4-20. This delay led to an artificial enhancement of the affinity of 4-4-20 for fluorescyl ligand. Utilization of a single chain derivative of 4-4-20 confirmed that anti-metatype reactivity was variable-region specific. Additionally, anti-metatype antibodies reacted with members of the 4-4-20 idiotype family, demonstrating varying degrees of affinity enhancement with idiotypically related molecules.","Anti-metatype antibodies significantly delayed dissociation of fluorescein structural analogues from the active site of 4-4-20. Fluorescein 5-isothiocyanate and fluorescein 6-isothiocyanate were conjugated to carriers of increasing molecular weights to test whether anti-metatype antibodies could stabilize the liganded 4-4-20 molecule by binding at the mouth of the active site. Significant delays were also observed for these fluorescein-conjugated compounds in the presence of anti-metatype antibodies. These results suggest that the mechanism whereby anti-metatype antibodies stabilize the liganded 4-4-20 molecule cannot be attributed solely to steric hindrance of ligand release due to anti-metatype antibodies binding at the mouth of the active site. Solvent perturbation studies of 4-4-20 with deuterium oxide revealed a reduction in the dynamics of the entire 4-4-20 molecule in the presence of anti-metatype antibodies.","In an attempt to produce monoclonal anti-metatope antibodies, Armenian hamsters were immunized with both affinity-labeled and liganded 4-4-20. While no ligand-requiring anti-metatope antibodies were produced, seventeen monoclonal anti-4-4-20 antibodies were isolated. Hamster monoclonal antibodies were classified into 5 separate groups based on binding properties, including the ability of ligand to inhibit binding of anti-4-4-20 antibodies, binding to 4-4-20 idiotype family, binding to monoclonal antibody 04-01, and western blot analysis. Six of the seven non-ligand inhibitable monoclonal antibodies tested demonstrated the ability to enhance the affinity of 4-4-20 for its ligand. Additionally, two ligand inhibitable monoclonal antibodies demonstrated the unique ability to delay the rate of ligand association with 4-4-20. Results of studies with both polyclonal and monoclonal antibodies against the 4-4-20 variable domain demonstrate that this approach provides information about subtle structural differences between liganded and non-liganded antibodies, immunoglobulin molecules and their single-chain derivatives, and mutant and wild-type single-chain antibodies.","Made available in DSpace on 2014-12-17T23:15:37Z (GMT). No. of bitstreams: 1 9305728.pdf: 6063101 bytes, checksum: 1fba4fc61c86c15e3df6313d7289a0d6 (MD5) Previous issue date: 1992","Embargo set by: Seth Robbins for item 72692 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","U of I Only","150 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1992."]},{"key":"dc:title","label":"Title","values":["Characterization and Analysis of Anti-Metatype Antibodies"]}]}],"canonical_facts":{"dc:contributor":["Voss, Edward W., Jr."],"dc:creator":["Weidner, Karla Marie"],"dc:date":["2014-12-17T23:15:37Z","10000-01-01","1992"],"dc:description":["Immunizations of high affinity anti-fluorescein monoclonal antibody 4-4-20 affinity-labeled with fluorescein 5-isothiocyanate into rabbit elicited antibodies specific for the liganded conformation of 4-4-20. Termed anti-metatype antibodies, this polyclonal reagent also demonstrated the unique ability to delay the rate of dissociation of fluorescyl ligand from the active site of 4-4-20. This delay led to an artificial enhancement of the affinity of 4-4-20 for fluorescyl ligand. Utilization of a single chain derivative of 4-4-20 confirmed that anti-metatype reactivity was variable-region specific. Additionally, anti-metatype antibodies reacted with members of the 4-4-20 idiotype family, demonstrating varying degrees of affinity enhancement with idiotypically related molecules.","Anti-metatype antibodies significantly delayed dissociation of fluorescein structural analogues from the active site of 4-4-20. Fluorescein 5-isothiocyanate and fluorescein 6-isothiocyanate were conjugated to carriers of increasing molecular weights to test whether anti-metatype antibodies could stabilize the liganded 4-4-20 molecule by binding at the mouth of the active site. Significant delays were also observed for these fluorescein-conjugated compounds in the presence of anti-metatype antibodies. These results suggest that the mechanism whereby anti-metatype antibodies stabilize the liganded 4-4-20 molecule cannot be attributed solely to steric hindrance of ligand release due to anti-metatype antibodies binding at the mouth of the active site. Solvent perturbation studies of 4-4-20 with deuterium oxide revealed a reduction in the dynamics of the entire 4-4-20 molecule in the presence of anti-metatype antibodies.","In an attempt to produce monoclonal anti-metatope antibodies, Armenian hamsters were immunized with both affinity-labeled and liganded 4-4-20. While no ligand-requiring anti-metatope antibodies were produced, seventeen monoclonal anti-4-4-20 antibodies were isolated. Hamster monoclonal antibodies were classified into 5 separate groups based on binding properties, including the ability of ligand to inhibit binding of anti-4-4-20 antibodies, binding to 4-4-20 idiotype family, binding to monoclonal antibody 04-01, and western blot analysis. Six of the seven non-ligand inhibitable monoclonal antibodies tested demonstrated the ability to enhance the affinity of 4-4-20 for its ligand. Additionally, two ligand inhibitable monoclonal antibodies demonstrated the unique ability to delay the rate of ligand association with 4-4-20. Results of studies with both polyclonal and monoclonal antibodies against the 4-4-20 variable domain demonstrate that this approach provides information about subtle structural differences between liganded and non-liganded antibodies, immunoglobulin molecules and their single-chain derivatives, and mutant and wild-type single-chain antibodies.","Made available in DSpace on 2014-12-17T23:15:37Z (GMT). No. of bitstreams: 1 9305728.pdf: 6063101 bytes, checksum: 1fba4fc61c86c15e3df6313d7289a0d6 (MD5) Previous issue date: 1992","Embargo set by: Seth Robbins for item 72692 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","U of I Only","150 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1992."],"dc:identifier":["http://hdl.handle.net/2142/72524","(UMI)AAI9305728"],"dc:subject":["Chemistry, Biochemistry","Health Sciences, Immunology"],"dc:title":["Characterization and Analysis of Anti-Metatype Antibodies"],"dc:type":["text"],"thesis:degree_discipline":["Microbiology"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:26:07Z"}