{"id":{"repo_id":"u-pacific","oai_identifier":"oai:scholarlycommons.pacific.edu:uop_etds-1516"},"canonical_url":"https://search.dev.ndltd.org/etd/u-pacific/oai:scholarlycommons.pacific.edu:uop_etds-1516","repository":{"repo_id":"u-pacific","name":"University of the Pacific","base_url":"https://scholarlycommons.pacific.edu/do/oai/"},"display":{"title":"Binding study of nickel complex to protein by equilibrium dialysis","abstract":"<p>A pyridine-containing Schiff base complex, 2, 12-dimethyl-3,7, 11 ,17- tetraazabicyclo( 11.3 .1 )-heptadeca-1 ( 17),2, 11 ,13, 15-pentaene, was chosen as the complex in this study based on previous studies that showed it to be the most active complex among a series of square planar nickel complexes in promoting DNA oxidation. This complex was synthesized and its structure was proven by electrospray mass spectroscopy, H-NMR, and elemental analysis. The H-NMR data also demonstrated that this complex has two vacant coordination sites in the distorted octahedral form in aqueous solution.</p> <p>Histone and bovine serum albumin which are typical proteins in eukaryote animals were chosen as the target materials when I studied whether this nickel complex could bind to proteins in the body. Nickel complex was labeled with Ni63 during the dialysis, and counted by a liquid scintillation counter.</p>","abstract_html":"&lt;p&gt;A pyridine-containing Schiff base complex, 2, 12-dimethyl-3,7, 11 ,17- tetraazabicyclo( 11.3 .1 )-heptadeca-1 ( 17),2, 11 ,13, 15-pentaene, was chosen as the complex in this study based on previous studies that showed it to be the most active complex among a series of square planar nickel complexes in promoting DNA oxidation. This complex was synthesized and its structure was proven by electrospray mass spectroscopy, H-NMR, and elemental analysis. The H-NMR data also demonstrated that this complex has two vacant coordination sites in the distorted octahedral form in aqueous solution.&lt;/p&gt; &lt;p&gt;Histone and bovine serum albumin which are typical proteins in eukaryote animals were chosen as the target materials when I studied whether this nickel complex could bind to proteins in the body. Nickel complex was labeled with Ni63 during the dialysis, and counted by a liquid scintillation counter.&lt;/p&gt;","abstract_has_math":false,"creators":["Zhou, Li"],"institution":null,"degree_name":"Master of Science (M.S.)","degree_level":"Thesis - Pacific Access Restricted","degree_discipline":"Chemistry","degree_department":null,"school":null,"contributors":["Patrick R. Jones"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":1998,"date_issued":"1998-01-01T08:00:00Z","date_published":"1998-01-01T08:00:00Z","updated_at":"2026-07-24T05:36:28Z","subjects":["Nickel","Nickel compounds","Proteins","Protein binding","Chemistry","Physical Sciences and Mathematics"],"languages":[],"rights":[],"rights_urls":["http://rightsstatements.org/vocab/InC/1.0/"],"identifier_entries":[]},"links":{"outbound_url":"https://scholarlycommons.pacific.edu/uop_etds/517","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Patrick R. 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This complex was synthesized and its structure was proven by electrospray mass spectroscopy, H-NMR, and elemental analysis. The H-NMR data also demonstrated that this complex has two vacant coordination sites in the distorted octahedral form in aqueous solution.</p> <p>Histone and bovine serum albumin which are typical proteins in eukaryote animals were chosen as the target materials when I studied whether this nickel complex could bind to proteins in the body. Nickel complex was labeled with Ni63 during the dialysis, and counted by a liquid scintillation counter.</p>"]},{"key":"dc:source","label":"Dc Source","values":["115"]},{"key":"dc:title","label":"Title","values":["Binding study of nickel complex to protein by equilibrium dialysis"]}]}],"canonical_facts":{"dc:contributor":["Patrick R. Jones"],"dc:creator":["Zhou, Li"],"dc:date.available":["2018-06-29T09:00:53Z"],"dc:description.abstract":["<p>A pyridine-containing Schiff base complex, 2, 12-dimethyl-3,7, 11 ,17- tetraazabicyclo( 11.3 .1 )-heptadeca-1 ( 17),2, 11 ,13, 15-pentaene, was chosen as the complex in this study based on previous studies that showed it to be the most active complex among a series of square planar nickel complexes in promoting DNA oxidation. This complex was synthesized and its structure was proven by electrospray mass spectroscopy, H-NMR, and elemental analysis. The H-NMR data also demonstrated that this complex has two vacant coordination sites in the distorted octahedral form in aqueous solution.</p> <p>Histone and bovine serum albumin which are typical proteins in eukaryote animals were chosen as the target materials when I studied whether this nickel complex could bind to proteins in the body. Nickel complex was labeled with Ni63 during the dialysis, and counted by a liquid scintillation counter.</p>"],"dc:identifier":["https://scholarlycommons.pacific.edu/uop_etds/517"],"dc:rights":["http://rightsstatements.org/vocab/InC/1.0/"],"dc:source":["115"],"dc:subject":["Nickel","Nickel compounds","Proteins","Protein binding","Chemistry","Physical Sciences and Mathematics"],"dc:title":["Binding study of nickel complex to protein by equilibrium dialysis"],"thesis:degree_discipline":["Chemistry"],"thesis:degree_level":["Thesis - Pacific Access Restricted"],"thesis:degree_name":["Master of Science (M.S.)"]},"updated_at":"2026-07-24T05:36:28Z"}