{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/84986"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/84986","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Betaine-Homocysteine Methyltransferase: Tissue Distribution, Nutrient Regulation, Genomic Organization, and Promoter Isolation","abstract":"The electrophoretic mobility (45 kDa) and the nucleotide sequence of the human kidney BHMT has been shown to be identical to liver BHMT. Initial rate data was plotted according to the method of Hanes and the Michaelis Constants were estimated to be 2160 muM and <10 muM for betaine and L-Homocysteine, respectively. These constants were same as the published human liver BHMT constants. Thus, we conclude that kidney and liver BHMT proteins are the product of one human BHMT gene.","abstract_html":"The electrophoretic mobility (45 kDa) and the nucleotide sequence of the human kidney BHMT has been shown to be identical to liver BHMT. Initial rate data was plotted according to the method of Hanes and the Michaelis Constants were estimated to be 2160 muM and &lt;10 muM for betaine and L-Homocysteine, respectively. These constants were same as the published human liver BHMT constants. Thus, we conclude that kidney and liver BHMT proteins are the product of one human BHMT gene.","abstract_has_math":false,"creators":["Park, Eric Inki"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Nutritional Sciences","degree_department":null,"school":null,"contributors":["Garrow, Timothy A."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-25T22:31:13Z","date_published":"2015-09-25T22:31:13Z","updated_at":"2026-07-22T22:26:24Z","subjects":["Biology, Molecular"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI9953104"],"render_values":[{"text":"(MiAaPQ)AAI9953104","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/84986","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Garrow, Timothy A."]},{"key":"dc:creator","label":"Author","values":["Park, Eric Inki"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-25T22:31:13Z","10000-01-01","1999"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Nutritional Sciences"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Illinois at Urbana-Champaign"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Biology, Molecular"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/84986","(MiAaPQ)AAI9953104"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["The electrophoretic mobility (45 kDa) and the nucleotide sequence of the human kidney BHMT has been shown to be identical to liver BHMT. Initial rate data was plotted according to the method of Hanes and the Michaelis Constants were estimated to be 2160 muM and <10 muM for betaine and L-Homocysteine, respectively. These constants were same as the published human liver BHMT constants. Thus, we conclude that kidney and liver BHMT proteins are the product of one human BHMT gene.","Made available in DSpace on 2015-09-25T22:31:13Z (GMT). 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Initial rate data was plotted according to the method of Hanes and the Michaelis Constants were estimated to be 2160 muM and <10 muM for betaine and L-Homocysteine, respectively. These constants were same as the published human liver BHMT constants. Thus, we conclude that kidney and liver BHMT proteins are the product of one human BHMT gene.","Made available in DSpace on 2015-09-25T22:31:13Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 9953104.pdf: 6224808 bytes, checksum: e466e42c05cb1311a5d86b1ab57c46a9 (MD5) Previous issue date: 1999","Embargo set by: Seth Robbins for item 86267 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","U of I Only","109 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1999."],"dc:identifier":["http://hdl.handle.net/2142/84986","(MiAaPQ)AAI9953104"],"dc:language":["eng"],"dc:subject":["Biology, Molecular"],"dc:title":["Betaine-Homocysteine Methyltransferase: Tissue Distribution, Nutrient Regulation, Genomic Organization, and Promoter Isolation"],"dc:type":["text"],"thesis:degree_discipline":["Nutritional Sciences"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:26:24Z"}