{"id":{"repo_id":"vu-aus","oai_identifier":"oai:eprints.vu.edu.au:15621"},"canonical_url":"https://search.dev.ndltd.org/etd/vu-aus/oai:eprints.vu.edu.au:15621","repository":{"repo_id":"vu-aus","name":"Victoria University (Australia)","base_url":"https://vuir.vu.edu.au/cgi/oai2"},"display":{"title":"Production of poly(adenosine diphosphate-ribose) polymerase-1: development of an efficient production and purification protocol","abstract":"PARP-1 is a nuclear enzyme involved in a range of activities associated with DNA metabolism, playing a key role in maintaining the integrity of DNA and chromatin structure. As such, this enzyme is likely to provide a useful target when using a rationale drug design approach to develop pharmaceutical reagents including cancer therapeutics. A major obstacle to this work however is that our knowledge of the relationship between structure and function of PARP-1 is rather limited. Structure - function studies of enzymes typically require the application of techniques for producing reasonable quantities of high quality protein. To this end, this thesis describes the development of a rapid and relatively simple approach to producing and purifying PARP-1.","abstract_html":"PARP-1 is a nuclear enzyme involved in a range of activities associated with DNA metabolism, playing a key role in maintaining the integrity of DNA and chromatin structure. As such, this enzyme is likely to provide a useful target when using a rationale drug design approach to develop pharmaceutical reagents including cancer therapeutics. A major obstacle to this work however is that our knowledge of the relationship between structure and function of PARP-1 is rather limited. Structure - function studies of enzymes typically require the application of techniques for producing reasonable quantities of high quality protein. To this end, this thesis describes the development of a rapid and relatively simple approach to producing and purifying PARP-1.","abstract_has_math":false,"creators":["Knight, Matthew"],"institution":"Victoria University of Technology","degree_name":"phd","degree_level":"doctoral","degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2003,"date_issued":"2003","date_published":"2003","updated_at":"2026-07-24T06:33:15Z","subjects":["0601 Biochemistry and Cell Biology","School of Engineering and Science","0304 Medicinal and Bimolecular Chemistry"],"languages":["en"],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":null,"outbound_label":null,"outbound_source":null},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["Knight, Matthew"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2003"]},{"key":"dc:date.issued","label":"Date","values":["2003"]},{"key":"dc:publisher.department","label":"Dc Publisher Department","values":["Unit for Food Safety, Authenticity and Quality"]},{"key":"dc:publisher.institution","label":"Dc Publisher Institution","values":["Victoria University of Technology"]},{"key":"dc:relation.isreferencedby","label":"Dc Relation Isreferencedby","values":["https://vuir.vu.edu.au/15621/"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]},{"key":"dc:type.qualificationlevel","label":"Dc Type Qualificationlevel","values":["doctoral"]},{"key":"dc:type.qualificationname","label":"Dc Type Qualificationname","values":["phd"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["0601 Biochemistry and Cell Biology","School of Engineering and Science","0304 Medicinal and Bimolecular Chemistry"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["en"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://vuir.vu.edu.au/15621/3/KNIGHT%20Matthew-thesis_nosignature.pdf"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["PARP-1 is a nuclear enzyme involved in a range of activities associated with DNA metabolism, playing a key role in maintaining the integrity of DNA and chromatin structure. As such, this enzyme is likely to provide a useful target when using a rationale drug design approach to develop pharmaceutical reagents including cancer therapeutics. A major obstacle to this work however is that our knowledge of the relationship between structure and function of PARP-1 is rather limited. Structure - function studies of enzymes typically require the application of techniques for producing reasonable quantities of high quality protein. To this end, this thesis describes the development of a rapid and relatively simple approach to producing and purifying PARP-1."]},{"key":"dc:format","label":"Dc Format","values":["text"]},{"key":"dc:title","label":"Title","values":["Production of poly(adenosine diphosphate-ribose) polymerase-1: development of an efficient production and purification protocol"]}]}],"canonical_facts":{"dc:creator":["Knight, Matthew"],"dc:date":["2003"],"dc:date.issued":["2003"],"dc:description.abstract":["PARP-1 is a nuclear enzyme involved in a range of activities associated with DNA metabolism, playing a key role in maintaining the integrity of DNA and chromatin structure. As such, this enzyme is likely to provide a useful target when using a rationale drug design approach to develop pharmaceutical reagents including cancer therapeutics. A major obstacle to this work however is that our knowledge of the relationship between structure and function of PARP-1 is rather limited. 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