Oxidation of 2-keto-4-hydroxyglutarate by pig heart and Escherichia coli [alpha]-ketoglutarate dehydrogenase complex
dc.contributor.author | Gupta, Subhash C. | en_US |
dc.contributor.author | Dekker, Eugene E. | en_US |
dc.date.accessioned | 2006-04-07T17:39:36Z | |
dc.date.available | 2006-04-07T17:39:36Z | |
dc.date.issued | 1979-01 | en_US |
dc.identifier.citation | Gupta, Subhash C., Dekker, Eugene E. (1979/01)."Oxidation of 2-keto-4-hydroxyglutarate by pig heart and Escherichia coli [alpha]-ketoglutarate dehydrogenase complex." Archives of Biochemistry and Biophysics 192(1): 324-326. <http://hdl.handle.net/2027.42/23715> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6WB5-4DW2M8X-2B6/2/df7d8f91313ce4f465f204dc7e81bf31 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/23715 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=373631&dopt=citation | en_US |
dc.description.abstract | Enzyme preparations from pig heart and Escherichia coli have been found to catalyze a NAD+- and CoASH-dependent oxidation of 2-keto-4-hydroxyglutarate. Several independent lines of evidence indicate that 2-keto-4-hydroxyglutarate is a substrate for the well-known [alpha]-ketoglutarate dehydrogenase complex of the citric acid cycle. The evidence includes (a) a constant ratio of specific activity values for the two substrates throughout purification, (b) identical elution profiles from a Ca3(PO4)2 gel-cellulose column, (c) the same sucrose density sedimentation patterns, (d) similar responses in controlled heat inactivation studies, and (e) identical pH-activity curves. | en_US |
dc.format.extent | 269565 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 | Oxidation of 2-keto-4-hydroxyglutarate by pig heart and Escherichia coli [alpha]-ketoglutarate dehydrogenase complex | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Public Health | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbsecondlevel | Biological Chemistry | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry The University of Michigan, Ann Arbor, Michigan 48109, U.S.A. | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry The University of Michigan, Ann Arbor, Michigan 48109, U.S.A. | en_US |
dc.identifier.pmid | 373631 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/23715/1/0000687.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0003-9861(79)90099-7 | en_US |
dc.identifier.source | Archives of Biochemistry and Biophysics | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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