{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/70502"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/70502","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Amino Acid Sequence Studies on the Beta Subunit of Bacterial Luciferase","abstract":"Peptides comprising 80% of the amino acid sequence of the (beta) subunit of bacterial luciferase from Vibrio harveyi were isolated and their amino acid sequences were determined by Edman degradation. The protein was fragmented by digestion with S. aureus V8 protease, trypsin, trypsin after citraconylation, and by treatment with cyanogen bromide. A substantial proportion of each peptide mixture precipitated and was not amenable to separation. Peptides were isolated by gel filbration, ion exchange chromatography, paper electrophoresis, and high performance reverse phase liquid chromatography. We have found no significant similarity between the (alpha) and (beta) subunits beyond their N-termini. We suggest that the N-terminal similarity may have some role in the function of the protein. Moreover, the (beta) subunit displays no sequence similarity to other flavoproteins, including regions and residues implicated in flavin binding by these enzymes. Therefore, our data do not suggest a role for the (beta) subunit in binding reduced flavin mononucleotide, but they do support the view that luciferase is significantly different from all other flavin monoxygenases.","abstract_html":"Peptides comprising 80% of the amino acid sequence of the (beta) subunit of bacterial luciferase from Vibrio harveyi were isolated and their amino acid sequences were determined by Edman degradation. The protein was fragmented by digestion with S. aureus V8 protease, trypsin, trypsin after citraconylation, and by treatment with cyanogen bromide. A substantial proportion of each peptide mixture precipitated and was not amenable to separation. Peptides were isolated by gel filbration, ion exchange chromatography, paper electrophoresis, and high performance reverse phase liquid chromatography. We have found no significant similarity between the (alpha) and (beta) subunits beyond their N-termini. We suggest that the N-terminal similarity may have some role in the function of the protein. Moreover, the (beta) subunit displays no sequence similarity to other flavoproteins, including regions and residues implicated in flavin binding by these enzymes. Therefore, our data do not suggest a role for the (beta) subunit in binding reduced flavin mononucleotide, but they do support the view that luciferase is significantly different from all other flavin monoxygenases.","abstract_has_math":false,"creators":["Thompson, Richard Blair"],"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":"2014-12-15T23:43:24Z","date_published":"2014-12-15T23:43:24Z","updated_at":"2026-07-22T22:26:03Z","subjects":["Chemistry, Biochemistry"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(UMI)AAI8203615"],"render_values":[{"text":"(UMI)AAI8203615","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/70502","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["Thompson, Richard Blair"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2014-12-15T23:43:24Z","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":["Chemistry, Biochemistry"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/70502","(UMI)AAI8203615"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Peptides comprising 80% of the amino acid sequence of the (beta) subunit of bacterial luciferase from Vibrio harveyi were isolated and their amino acid sequences were determined by Edman degradation. The protein was fragmented by digestion with S. aureus V8 protease, trypsin, trypsin after citraconylation, and by treatment with cyanogen bromide. A substantial proportion of each peptide mixture precipitated and was not amenable to separation. Peptides were isolated by gel filbration, ion exchange chromatography, paper electrophoresis, and high performance reverse phase liquid chromatography. We have found no significant similarity between the (alpha) and (beta) subunits beyond their N-termini. We suggest that the N-terminal similarity may have some role in the function of the protein. Moreover, the (beta) subunit displays no sequence similarity to other flavoproteins, including regions and residues implicated in flavin binding by these enzymes. Therefore, our data do not suggest a role for the (beta) subunit in binding reduced flavin mononucleotide, but they do support the view that luciferase is significantly different from all other flavin monoxygenases.","Made available in DSpace on 2014-12-15T23:43:24Z (GMT). No. of bitstreams: 1 8203615.pdf: 2993417 bytes, checksum: 2b835845c4a4db9d37f9dbbd61158e9c (MD5) Previous issue date: 1981","Embargo set by: Seth Robbins for item 70668 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","124 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1981."]},{"key":"dc:title","label":"Title","values":["Amino Acid Sequence Studies on the Beta Subunit of Bacterial Luciferase"]}]}],"canonical_facts":{"dc:creator":["Thompson, Richard Blair"],"dc:date":["2014-12-15T23:43:24Z","10000-01-01","1981"],"dc:description":["Peptides comprising 80% of the amino acid sequence of the (beta) subunit of bacterial luciferase from Vibrio harveyi were isolated and their amino acid sequences were determined by Edman degradation. The protein was fragmented by digestion with S. aureus V8 protease, trypsin, trypsin after citraconylation, and by treatment with cyanogen bromide. A substantial proportion of each peptide mixture precipitated and was not amenable to separation. Peptides were isolated by gel filbration, ion exchange chromatography, paper electrophoresis, and high performance reverse phase liquid chromatography. We have found no significant similarity between the (alpha) and (beta) subunits beyond their N-termini. We suggest that the N-terminal similarity may have some role in the function of the protein. Moreover, the (beta) subunit displays no sequence similarity to other flavoproteins, including regions and residues implicated in flavin binding by these enzymes. Therefore, our data do not suggest a role for the (beta) subunit in binding reduced flavin mononucleotide, but they do support the view that luciferase is significantly different from all other flavin monoxygenases.","Made available in DSpace on 2014-12-15T23:43:24Z (GMT). No. of bitstreams: 1 8203615.pdf: 2993417 bytes, checksum: 2b835845c4a4db9d37f9dbbd61158e9c (MD5) Previous issue date: 1981","Embargo set by: Seth Robbins for item 70668 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","124 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1981."],"dc:identifier":["http://hdl.handle.net/2142/70502","(UMI)AAI8203615"],"dc:subject":["Chemistry, Biochemistry"],"dc:title":["Amino Acid Sequence Studies on the Beta Subunit of Bacterial Luciferase"],"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":"2026-07-22T22:26:03Z"}