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Oxidation of 2-keto-4-hydroxyglutarate by pig heart and Escherichia coli [alpha]-ketoglutarate dehydrogenase complex

dc.contributor.authorGupta, Subhash C.en_US
dc.contributor.authorDekker, Eugene E.en_US
dc.date.accessioned2006-04-07T17:39:36Z
dc.date.available2006-04-07T17:39:36Z
dc.date.issued1979-01en_US
dc.identifier.citationGupta, 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.urihttp://www.sciencedirect.com/science/article/B6WB5-4DW2M8X-2B6/2/df7d8f91313ce4f465f204dc7e81bf31en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/23715
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=373631&dopt=citationen_US
dc.description.abstractEnzyme 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.extent269565 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleOxidation of 2-keto-4-hydroxyglutarate by pig heart and Escherichia coli [alpha]-ketoglutarate dehydrogenase complexen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelPublic Healthen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Biological Chemistry The University of Michigan, Ann Arbor, Michigan 48109, U.S.A.en_US
dc.contributor.affiliationumDepartment of Biological Chemistry The University of Michigan, Ann Arbor, Michigan 48109, U.S.A.en_US
dc.identifier.pmid373631en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/23715/1/0000687.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0003-9861(79)90099-7en_US
dc.identifier.sourceArchives of Biochemistry and Biophysicsen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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