{"id":{"repo_id":"ohiolink","oai_identifier":"oai:etd.ohiolink.edu:ysu1355527551"},"canonical_url":"https://search.dev.ndltd.org/etd/ohiolink/oai:etd.ohiolink.edu:ysu1355527551","repository":{"repo_id":"ohiolink","name":"OhioLINK","base_url":"https://etd.ohiolink.edu/acprod/odb_etd/ws/oai/oai"},"display":{"title":"Cloning and Overexpression of Yeast Cystathionine γ-Lyase","abstract":"Cystathionine γ-lyase (CGL) is a protein involved in the conversion of methionine to cysteine as part of the trans-sulfuration pathway. Inactivation of the enzyme, possibly by oxidation of reactive site residues, has been linked to cataractogenesis. This research isolated the cystathionine γ-lyase gene (<i>CYS3</i>), modified it with an XhoI and BlpI restriction site and enterokinase sequence (creating a modified <i>CYS3</i>, <i>mCYS3</i>, gene), and ultimately spliced it into a pET-15b plasmid to create a recombinant plasmid. Then transformed the recombinant plasmid into BL21 E. coli cells. This enabled the production of bacterial cells capable of generating µg amounts of CGL for future metal catalyzed oxidation (MCO) research.","abstract_html":"Cystathionine γ-lyase (CGL) is a protein involved in the conversion of methionine to cysteine as part of the trans-sulfuration pathway. Inactivation of the enzyme, possibly by oxidation of reactive site residues, has been linked to cataractogenesis. This research isolated the cystathionine γ-lyase gene (&lt;i&gt;CYS3&lt;/i&gt;), modified it with an XhoI and BlpI restriction site and enterokinase sequence (creating a modified &lt;i&gt;CYS3&lt;/i&gt;, &lt;i&gt;mCYS3&lt;/i&gt;, gene), and ultimately spliced it into a pET-15b plasmid to create a recombinant plasmid. Then transformed the recombinant plasmid into BL21 E. coli cells. This enabled the production of bacterial cells capable of generating µg amounts of CGL for future metal catalyzed oxidation (MCO) research.","abstract_has_math":false,"creators":["Raby, Roger Lee, Jr."],"institution":"Youngstown State University","degree_name":"Master of Science in Chemistry","degree_level":"masters","degree_discipline":"Department of Chemistry","degree_department":null,"school":null,"contributors":["Serra, Michael"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2012,"date_issued":"2012","date_published":"2012","updated_at":"2026-07-24T03:36:39Z","subjects":["Biochemistry","Chemistry","cloning","overexpression","cataractogenesis","cystahionine gamma-lyase","enterokinase","plasmid","cystathionine"],"languages":["English"],"rights":["unrestricted","This thesis or dissertation is protected by copyright: all rights reserved. It may not be copied or redistributed beyond the terms of applicable copyright laws."],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://rave.ohiolink.edu/etdc/view?acc_num=ysu1355527551","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Serra, Michael"]},{"key":"dc:creator","label":"Author","values":["Raby, Roger Lee, Jr."]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2012"]},{"key":"dc:publisher","label":"Institution","values":["Youngstown State University / OhioLINK"]},{"key":"dc:type","label":"Dc Type","values":["Electronic Thesis or Dissertation"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Department of Chemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["masters"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Master of Science in Chemistry"]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["Youngstown State University"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Biochemistry","Chemistry","cloning","overexpression","cataractogenesis","cystahionine gamma-lyase","enterokinase","plasmid","cystathionine"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["English"]},{"key":"dc:rights","label":"Dc Rights","values":["unrestricted","This thesis or dissertation is protected by copyright: all rights reserved. It may not be copied or redistributed beyond the terms of applicable copyright laws."]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://rave.ohiolink.edu/etdc/view?acc_num=ysu1355527551"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Cystathionine γ-lyase (CGL) is a protein involved in the conversion of methionine to cysteine as part of the trans-sulfuration pathway. Inactivation of the enzyme, possibly by oxidation of reactive site residues, has been linked to cataractogenesis. This research isolated the cystathionine γ-lyase gene (<i>CYS3</i>), modified it with an XhoI and BlpI restriction site and enterokinase sequence (creating a modified <i>CYS3</i>, <i>mCYS3</i>, gene), and ultimately spliced it into a pET-15b plasmid to create a recombinant plasmid. Then transformed the recombinant plasmid into BL21 E. coli cells. This enabled the production of bacterial cells capable of generating µg amounts of CGL for future metal catalyzed oxidation (MCO) research."]},{"key":"dc:format","label":"Dc Format","values":["application/pdf","p.56","862.3 KB"]},{"key":"dc:title","label":"Title","values":["Cloning and Overexpression of Yeast Cystathionine γ-Lyase"]}]}],"canonical_facts":{"dc:contributor":["Serra, Michael"],"dc:creator":["Raby, Roger Lee, Jr."],"dc:date":["2012"],"dc:description":["Cystathionine γ-lyase (CGL) is a protein involved in the conversion of methionine to cysteine as part of the trans-sulfuration pathway. Inactivation of the enzyme, possibly by oxidation of reactive site residues, has been linked to cataractogenesis. This research isolated the cystathionine γ-lyase gene (<i>CYS3</i>), modified it with an XhoI and BlpI restriction site and enterokinase sequence (creating a modified <i>CYS3</i>, <i>mCYS3</i>, gene), and ultimately spliced it into a pET-15b plasmid to create a recombinant plasmid. Then transformed the recombinant plasmid into BL21 E. coli cells. This enabled the production of bacterial cells capable of generating µg amounts of CGL for future metal catalyzed oxidation (MCO) research."],"dc:format":["application/pdf","p.56","862.3 KB"],"dc:identifier":["http://rave.ohiolink.edu/etdc/view?acc_num=ysu1355527551"],"dc:language":["English"],"dc:publisher":["Youngstown State University / OhioLINK"],"dc:rights":["unrestricted","This thesis or dissertation is protected by copyright: all rights reserved. It may not be copied or redistributed beyond the terms of applicable copyright laws."],"dc:subject":["Biochemistry","Chemistry","cloning","overexpression","cataractogenesis","cystahionine gamma-lyase","enterokinase","plasmid","cystathionine"],"dc:title":["Cloning and Overexpression of Yeast Cystathionine γ-Lyase"],"dc:type":["Electronic Thesis or Dissertation"],"thesis:degree_discipline":["Department of Chemistry"],"thesis:degree_level":["masters"],"thesis:degree_name":["Master of Science in Chemistry"],"thesis:institution_name":["Youngstown State University"]},"updated_at":"2026-07-24T03:36:39Z"}