A possible role in the regulation of primary amination for a complex of glutamine: [alpha]-Ketoglutarate amidotransferase and glutamate dehydrogenase in
dc.contributor.author | Savageau, Michael A. | en_US |
dc.contributor.author | Kotre, Ann Marie | en_US |
dc.contributor.author | Sakamoto, Naoto | en_US |
dc.date.accessioned | 2006-04-17T16:48:00Z | |
dc.date.available | 2006-04-17T16:48:00Z | |
dc.date.issued | 1972-07-11 | en_US |
dc.identifier.citation | Savageau, Michael A., Kotre, Ann Marie, Sakamoto, Naoto (1972/07/11)."A possible role in the regulation of primary amination for a complex of glutamine: [alpha]-Ketoglutarate amidotransferase and glutamate dehydrogenase in." Biochemical and Biophysical Research Communications 48(1): 41-47. <http://hdl.handle.net/2027.42/34071> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6WBK-4DYM9YK-1FN/2/78a9619367fc930a0f5a7bc5f67e08e3 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/34071 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=4557512&dopt=citation | en_US |
dc.description.abstract | Both glutamine: [alpha]-ketoglutarate amidotransferase and glutamate dehydrogenase activities are obtained from grown in minimal medium containing glucose and ammonia. These activities are not additive, suggesting an interaction between them. Normally both of these activities are equally inhibited by homoserine. In mutants resistant to homoserine inhibition both activities are affected in parallel. Furthermore, the ratio of the wild-type activities remains constant over a 30-fold range in purification. This evidence suggests that these activities are associated with a single complex. A possible role for this complex in the regulation of primary amination is discussed. | en_US |
dc.format.extent | 362307 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | A possible role in the regulation of primary amination for a complex of glutamine: [alpha]-Ketoglutarate amidotransferase and glutamate dehydrogenase in | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Natural Resources and Environment | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbsecondlevel | Ecology and Evolutionary Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Microbiology, University of Michigan, Ann Arbor, Michigan 48104, USA | en_US |
dc.contributor.affiliationum | Department of Microbiology, University of Michigan, Ann Arbor, Michigan 48104, USA | en_US |
dc.contributor.affiliationum | Department of Microbiology, University of Michigan, Ann Arbor, Michigan 48104, USA | en_US |
dc.identifier.pmid | 4557512 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/34071/1/0000349.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0006-291X(72)90341-5 | en_US |
dc.identifier.source | Biochemical and Biophysical Research Communications | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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