{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/67410"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/67410","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"A Study of the Inactivation in Vivo of the Luciferase in the Luminous Marine Bacterium Beneckea Harveyi","abstract":"The inactivation in vivo of the luciferase in stationary phase cultures of the luminous marine bacterium Beneckea harveyi was studied in an effort to elucidate its mechanism. Through studies utilizing inhibitors of metabolic energy production, an inhibitor of protein synthesis, and a mutant in which the luciferase was inactivated at a much slower rate, and through studies of intracellular ATP levels under various conditions, a model for the modulation of luciferase inactivation by a signal metabolite or metabolites of as yet unknown chemical identity was developed, and degradation of the luciferase to its constituent amino acids was ruled out as the direct cause of the inactivation. In a preliminary immunochemical study of the inactivation process, no inactive anti-luciferase cross-reacting material could be detected at any point during the inactivation under any conditions, suggesting that inactivated luciferase is in a form which is unrecognizable by antibodies directed against the native enzyme.","abstract_html":"The inactivation in vivo of the luciferase in stationary phase cultures of the luminous marine bacterium Beneckea harveyi was studied in an effort to elucidate its mechanism. Through studies utilizing inhibitors of metabolic energy production, an inhibitor of protein synthesis, and a mutant in which the luciferase was inactivated at a much slower rate, and through studies of intracellular ATP levels under various conditions, a model for the modulation of luciferase inactivation by a signal metabolite or metabolites of as yet unknown chemical identity was developed, and degradation of the luciferase to its constituent amino acids was ruled out as the direct cause of the inactivation. In a preliminary immunochemical study of the inactivation process, no inactive anti-luciferase cross-reacting material could be detected at any point during the inactivation under any conditions, suggesting that inactivated luciferase is in a form which is unrecognizable by antibodies directed against the native enzyme.","abstract_has_math":false,"creators":["Reeve, Carole Anne"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Biochemistry","degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2014,"date_issued":"2014-12-14T04:27:56Z","date_published":"2014-12-14T04:27:56Z","updated_at":"2026-07-22T22:25:57Z","subjects":["Biology, Microbiology"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(UMI)AAI8114467"],"render_values":[{"text":"(UMI)AAI8114467","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/67410","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["Reeve, Carole Anne"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2014-12-14T04:27:56Z","10000-01-01","1981"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biochemistry"]},{"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":["Biology, Microbiology"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/67410","(UMI)AAI8114467"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["The inactivation in vivo of the luciferase in stationary phase cultures of the luminous marine bacterium Beneckea harveyi was studied in an effort to elucidate its mechanism. Through studies utilizing inhibitors of metabolic energy production, an inhibitor of protein synthesis, and a mutant in which the luciferase was inactivated at a much slower rate, and through studies of intracellular ATP levels under various conditions, a model for the modulation of luciferase inactivation by a signal metabolite or metabolites of as yet unknown chemical identity was developed, and degradation of the luciferase to its constituent amino acids was ruled out as the direct cause of the inactivation. In a preliminary immunochemical study of the inactivation process, no inactive anti-luciferase cross-reacting material could be detected at any point during the inactivation under any conditions, suggesting that inactivated luciferase is in a form which is unrecognizable by antibodies directed against the native enzyme.","Made available in DSpace on 2014-12-14T04:27:56Z (GMT). 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Through studies utilizing inhibitors of metabolic energy production, an inhibitor of protein synthesis, and a mutant in which the luciferase was inactivated at a much slower rate, and through studies of intracellular ATP levels under various conditions, a model for the modulation of luciferase inactivation by a signal metabolite or metabolites of as yet unknown chemical identity was developed, and degradation of the luciferase to its constituent amino acids was ruled out as the direct cause of the inactivation. In a preliminary immunochemical study of the inactivation process, no inactive anti-luciferase cross-reacting material could be detected at any point during the inactivation under any conditions, suggesting that inactivated luciferase is in a form which is unrecognizable by antibodies directed against the native enzyme.","Made available in DSpace on 2014-12-14T04:27:56Z (GMT). No. of bitstreams: 1 8114467.pdf: 6630809 bytes, checksum: 5cdae68abb81a2e69ceb45f5c2233dc7 (MD5) Previous issue date: 1981","Embargo set by: Seth Robbins for item 67588 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","182 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1981."],"dc:identifier":["http://hdl.handle.net/2142/67410","(UMI)AAI8114467"],"dc:language":["eng"],"dc:subject":["Biology, Microbiology"],"dc:title":["A Study of the Inactivation in Vivo of the Luciferase in the Luminous Marine Bacterium Beneckea Harveyi"],"dc:type":["text"],"thesis:degree_discipline":["Biochemistry"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:25:57Z"}