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oai:www.ideals.illinois.edu:2142/84986 2023-07-11 col_2142_5131 col_2142_14797 com_2142_5130 com_2142_14796 com_2142_397

Garrow, Timothy A. Park, Eric Inki 2015-09-25T22:31:13Z 2015-09-25T22:31:13Z 10000-01-01 1999 1999 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). 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. http://hdl.handle.net/2142/84986 (MiAaPQ)AAI9953104 eng Biology, Molecular Betaine-Homocysteine Methyltransferase: Tissue Distribution, Nutrient Regulation, Genomic Organization, and Promoter Isolation text Nutritional Sciences Nutritional Sciences University of Illinois at Urbana-Champaign Dissertation Ph.D.