{"id":{"repo_id":"unt","oai_identifier":"info:ark/67531/metadc2864"},"canonical_url":"https://search.dev.ndltd.org/etd/unt/info:ark/67531/metadc2864","repository":{"repo_id":"unt","name":"University of North Texas","base_url":"https://digital.library.unt.edu/oai/"},"display":{"title":"Purification of Aspartate Transcarbamoylase from Moraxella (Branhamella) catarrhalis","abstract":"The enzyme, aspartate transcarbamoylase (ATCase) from Moraxella (Branhamella) catarrhalis, has been purified. The holoenzyme has a molecular mass of approximately 510kDa, harbors predominantly positive charges and is hydrophobic in nature. The holoenzyme possesses two subunits, a smaller one of 40 kDa and a larger one of 45 kDa. A third polypeptide has been found to contribute to the overall enzymatic activity, having an approximate mass of 55 kDa. The ATCase purification included the generation of cell-free extract, streptomycin sulfate cut, 60 °C heat step, ammonium sulfate cut, dialysis and ion, gel-filtration and hydrophobic interaction chromatography. The enzyme's performance throughout purification steps was analyzed on activity and SDS-PAGE gradient gels. Its enzymatic, specific activities, yield and fold purification, were also determined.","abstract_html":"The enzyme, aspartate transcarbamoylase (ATCase) from Moraxella (Branhamella) catarrhalis, has been purified. The holoenzyme has a molecular mass of approximately 510kDa, harbors predominantly positive charges and is hydrophobic in nature. The holoenzyme possesses two subunits, a smaller one of 40 kDa and a larger one of 45 kDa. A third polypeptide has been found to contribute to the overall enzymatic activity, having an approximate mass of 55 kDa. The ATCase purification included the generation of cell-free extract, streptomycin sulfate cut, 60 °C heat step, ammonium sulfate cut, dialysis and ion, gel-filtration and hydrophobic interaction chromatography. The enzyme's performance throughout purification steps was analyzed on activity and SDS-PAGE gradient gels. Its enzymatic, specific activities, yield and fold purification, were also determined.","abstract_has_math":false,"creators":["Stawska, Agnieszka A."],"institution":"University of North Texas","degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":["O'Donovan, Gerard A.","Benjamin, Robert C.","Zimmerman, Earl G."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2001,"date_issued":"2001-08","date_published":"2001-08","updated_at":"2026-07-24T05:34:52Z","subjects":["Pyrimidine nucleotides -- Metabolism.","Moraxella.","Moraxella catarrhalis","Aspartate transcarbamoylase","Subunits","Holoenzyme","Enzyme purification"],"languages":["English"],"rights":["Public","Copyright","Stawska, Agnieszka A.","Copyright is held by the author, unless otherwise noted. All rights reserved."],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["oclc: 51243955","https://digital.library.unt.edu/ark:/67531/metadc2864/","ark: ark:/67531/metadc2864"],"render_values":[{"text":"oclc: 51243955","href":null,"code":true},{"text":"https://digital.library.unt.edu/ark:/67531/metadc2864/","href":"https://digital.library.unt.edu/ark:/67531/metadc2864/","code":true},{"text":"ark: ark:/67531/metadc2864","href":null,"code":true}]}]},"links":{"outbound_url":"https://doi.org/10.12794/metadc2864","outbound_label":"DOI","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["O'Donovan, Gerard A.","Benjamin, Robert C.","Zimmerman, Earl G."]},{"key":"dc:creator","label":"Author","values":["Stawska, Agnieszka A."]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2001-08"]},{"key":"dc:publisher","label":"Institution","values":["University of North Texas"]},{"key":"dc:type","label":"Dc Type","values":["Thesis or Dissertation"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Pyrimidine nucleotides -- Metabolism.","Moraxella.","Moraxella catarrhalis","Aspartate transcarbamoylase","Subunits","Holoenzyme","Enzyme purification"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["English"]},{"key":"dc:rights","label":"Dc Rights","values":["Public","Copyright","Stawska, Agnieszka A.","Copyright is held by the author, unless otherwise noted. 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The ATCase purification included the generation of cell-free extract, streptomycin sulfate cut, 60 °C heat step, ammonium sulfate cut, dialysis and ion, gel-filtration and hydrophobic interaction chromatography. The enzyme's performance throughout purification steps was analyzed on activity and SDS-PAGE gradient gels. Its enzymatic, specific activities, yield and fold purification, were also determined."]},{"key":"dc:format","label":"Dc Format","values":["Text"]},{"key":"dc:title","label":"Title","values":["Purification of Aspartate Transcarbamoylase from Moraxella (Branhamella) catarrhalis"]}]}],"canonical_facts":{"dc:contributor":["O'Donovan, Gerard A.","Benjamin, Robert C.","Zimmerman, Earl G."],"dc:creator":["Stawska, Agnieszka A."],"dc:date":["2001-08"],"dc:description":["The enzyme, aspartate transcarbamoylase (ATCase) from Moraxella (Branhamella) catarrhalis, has been purified. The holoenzyme has a molecular mass of approximately 510kDa, harbors predominantly positive charges and is hydrophobic in nature. The holoenzyme possesses two subunits, a smaller one of 40 kDa and a larger one of 45 kDa. A third polypeptide has been found to contribute to the overall enzymatic activity, having an approximate mass of 55 kDa. The ATCase purification included the generation of cell-free extract, streptomycin sulfate cut, 60 °C heat step, ammonium sulfate cut, dialysis and ion, gel-filtration and hydrophobic interaction chromatography. The enzyme's performance throughout purification steps was analyzed on activity and SDS-PAGE gradient gels. 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