{"id":{"repo_id":"vt","oai_identifier":"oai:vtechworks.lib.vt.edu:10919/74553"},"canonical_url":"https://search.dev.ndltd.org/etd/vt/oai:vtechworks.lib.vt.edu:10919/74553","repository":{"repo_id":"vt","name":"Virginia Tech","base_url":"https://vtechworks.lib.vt.edu/oai/request"},"display":{"title":"Propionyl holocarboxylase synthesis","abstract":"A soluble enzyme system, isolated from livers of biotin-deficient rats, catalyzes the ATP-dependent synthesis of propionyl holocarboxylase from d-biotin and propionyl apocarboxylase. This system has been resolved by alumina C<sub>∂</sub> gel fractionation into two essential components; (a) gel supernatant which contains propionyl apocarboxylase and (b) gel eluate which contains an enzyme which catalyzes the covalent bonding of d-biotin to propionyl apocarboxylase. The propionyl holocarboxylase synthesis catalyzed by these enzyme systems is irreversible and d·biotin specific. The gel supernatant has been further purified by hydroxyapatite chromatography and (NH₄)₂SO₄ fractionation and the gel eluate by (NH₄)₂SO₄ precipitation and cellulose-phosphate chromatography. An enzyme similar to the gel eluate enzyme has been isolated from cell-free extracts of Propionibacterium shermanii. Although cell-free extracts of P. shermanii do not contain propionyl apo- or holocarboxylase, they do catalyze ATP-dependent propionyl holocarboxylase formation from d·biotin and rat liver propionyl apocarboxylase. Biotin-2'-C¹⁴-labelled propionyl holocarboxylaae, synthesized with these enzyme systems, does not transfer C¹⁴O₂ to propionyl-CoA indicating that the ureido carbon of enzyme-bound biotin is not the\"active carbon\" of biotin.","abstract_html":"A soluble enzyme system, isolated from livers of biotin-deficient rats, catalyzes the ATP-dependent synthesis of propionyl holocarboxylase from d-biotin and propionyl apocarboxylase. This system has been resolved by alumina C&lt;sub&gt;∂&lt;/sub&gt; gel fractionation into two essential components; (a) gel supernatant which contains propionyl apocarboxylase and (b) gel eluate which contains an enzyme which catalyzes the covalent bonding of d-biotin to propionyl apocarboxylase. The propionyl holocarboxylase synthesis catalyzed by these enzyme systems is irreversible and d·biotin specific. The gel supernatant has been further purified by hydroxyapatite chromatography and (NH₄)₂SO₄ fractionation and the gel eluate by (NH₄)₂SO₄ precipitation and cellulose-phosphate chromatography. An enzyme similar to the gel eluate enzyme has been isolated from cell-free extracts of Propionibacterium shermanii. Although cell-free extracts of P. shermanii do not contain propionyl apo- or holocarboxylase, they do catalyze ATP-dependent propionyl holocarboxylase formation from d·biotin and rat liver propionyl apocarboxylase. Biotin-2&#x27;-C¹⁴-labelled propionyl holocarboxylaae, synthesized with these enzyme systems, does not transfer C¹⁴O₂ to propionyl-CoA indicating that the ureido carbon of enzyme-bound biotin is not the&quot;active carbon&quot; of biotin.","abstract_has_math":false,"creators":["Huang, Shu Chin"],"institution":"Virginia Polytechnic Institute","degree_name":"Master of Science","degree_level":"masters","degree_discipline":"Biochemistry and Nutrition","degree_department":"Biochemistry and Nutrition","school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":1963,"date_issued":"1963","date_published":"1963","updated_at":"2026-07-22T22:19:35Z","subjects":[],"languages":["en_US"],"rights":["In Copyright"],"rights_urls":["http://rightsstatements.org/vocab/InC/1.0/"],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/10919/74553","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.department","label":"Department","values":["Biochemistry and Nutrition"]},{"key":"dc:creator","label":"Author","values":["Huang, Shu Chin"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2017-01-30T21:03:02Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2017-01-30T21:03:02Z"]},{"key":"dc:date.issued","label":"Date","values":["1963"]},{"key":"dc:publisher","label":"Institution","values":["Virginia Polytechnic Institute"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]},{"key":"dc:type.dcmitype","label":"Dc Type Dcmitype","values":["Text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biochemistry and Nutrition"]},{"key":"thesis:degree_level","label":"Degree Level","values":["masters"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Master of Science"]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["Virginia Polytechnic Institute"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language.iso","label":"Language (ISO)","values":["en_US"]},{"key":"dc:rights","label":"Dc Rights","values":["In Copyright"]},{"key":"dc:rights.uri","label":"Rights URI","values":["http://rightsstatements.org/vocab/InC/1.0/"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["http://hdl.handle.net/10919/74553"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["A soluble enzyme system, isolated from livers of biotin-deficient rats, catalyzes the ATP-dependent synthesis of propionyl holocarboxylase from d-biotin and propionyl apocarboxylase. This system has been resolved by alumina C<sub>∂</sub> gel fractionation into two essential components; (a) gel supernatant which contains propionyl apocarboxylase and (b) gel eluate which contains an enzyme which catalyzes the covalent bonding of d-biotin to propionyl apocarboxylase. The propionyl holocarboxylase synthesis catalyzed by these enzyme systems is irreversible and d·biotin specific. The gel supernatant has been further purified by hydroxyapatite chromatography and (NH₄)₂SO₄ fractionation and the gel eluate by (NH₄)₂SO₄ precipitation and cellulose-phosphate chromatography. An enzyme similar to the gel eluate enzyme has been isolated from cell-free extracts of Propionibacterium shermanii. Although cell-free extracts of P. shermanii do not contain propionyl apo- or holocarboxylase, they do catalyze ATP-dependent propionyl holocarboxylase formation from d·biotin and rat liver propionyl apocarboxylase. Biotin-2'-C¹⁴-labelled propionyl holocarboxylaae, synthesized with these enzyme systems, does not transfer C¹⁴O₂ to propionyl-CoA indicating that the ureido carbon of enzyme-bound biotin is not the\"active carbon\" of biotin."]},{"key":"dc:description.degree","label":"Dc Description Degree","values":["Master of Science"]},{"key":"dc:format.mimetype","label":"Dc Format Mimetype","values":["application/pdf"]},{"key":"dc:title","label":"Title","values":["Propionyl holocarboxylase synthesis"]}]}],"canonical_facts":{"dc:contributor.department":["Biochemistry and Nutrition"],"dc:creator":["Huang, Shu Chin"],"dc:date.accessioned":["2017-01-30T21:03:02Z"],"dc:date.available":["2017-01-30T21:03:02Z"],"dc:date.issued":["1963"],"dc:description.abstract":["A soluble enzyme system, isolated from livers of biotin-deficient rats, catalyzes the ATP-dependent synthesis of propionyl holocarboxylase from d-biotin and propionyl apocarboxylase. This system has been resolved by alumina C<sub>∂</sub> gel fractionation into two essential components; (a) gel supernatant which contains propionyl apocarboxylase and (b) gel eluate which contains an enzyme which catalyzes the covalent bonding of d-biotin to propionyl apocarboxylase. The propionyl holocarboxylase synthesis catalyzed by these enzyme systems is irreversible and d·biotin specific. The gel supernatant has been further purified by hydroxyapatite chromatography and (NH₄)₂SO₄ fractionation and the gel eluate by (NH₄)₂SO₄ precipitation and cellulose-phosphate chromatography. An enzyme similar to the gel eluate enzyme has been isolated from cell-free extracts of Propionibacterium shermanii. Although cell-free extracts of P. shermanii do not contain propionyl apo- or holocarboxylase, they do catalyze ATP-dependent propionyl holocarboxylase formation from d·biotin and rat liver propionyl apocarboxylase. Biotin-2'-C¹⁴-labelled propionyl holocarboxylaae, synthesized with these enzyme systems, does not transfer C¹⁴O₂ to propionyl-CoA indicating that the ureido carbon of enzyme-bound biotin is not the\"active carbon\" of biotin."],"dc:description.degree":["Master of Science"],"dc:format.mimetype":["application/pdf"],"dc:identifier.uri":["http://hdl.handle.net/10919/74553"],"dc:language.iso":["en_US"],"dc:publisher":["Virginia Polytechnic Institute"],"dc:rights":["In Copyright"],"dc:rights.uri":["http://rightsstatements.org/vocab/InC/1.0/"],"dc:title":["Propionyl holocarboxylase synthesis"],"dc:type":["Thesis"],"dc:type.dcmitype":["Text"],"thesis:degree_discipline":["Biochemistry and Nutrition"],"thesis:degree_level":["masters"],"thesis:degree_name":["Master of Science"],"thesis:institution_name":["Virginia Polytechnic Institute"]},"updated_at":"2026-07-22T22:19:35Z"}