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The chemical synthesis of 2-keto-3-deoxy-octonate and its cleavage by a specific aldolase
dc.contributor.authorGhalambor, Mohammad Alien_US
dc.contributor.authorHeath, Edward C.en_US
dc.date.accessioned2006-04-13T14:51:27Z
dc.date.available2006-04-13T14:51:27Z
dc.date.issued1963-05-22en_US
dc.identifier.citationGhalambor, Mohammad Ali, Heath, Edward C. (1963/05/22)."The chemical synthesis of 2-keto-3-deoxy-octonate and its cleavage by a specific aldolase." Biochemical and Biophysical Research Communications 11(4): 288-293. <http://hdl.handle.net/2027.42/32223>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6WBK-4DX4JMR-DY/2/72f2cf3e067161271360564e160a4ae3en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/32223
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=13960611&dopt=citationen_US
dc.description.abstractWe have previously reported (Heath and Ghalambor, 1963) the occurrence of 2-keto-3-deoxy-octonate (KDO) as a glycosidically-bound constituent of cell wall lipopolysaccharide (LPS) of 0111-B4 and the enzymatic synthesis of CMP-KDO (Ghalambor and Heath, 1963). This report presents evidence for the chemical synthesis of KDO and its enzymatic cleavage (KDO-aldolase) to yield equimolar quantities of pyruvate and D-arabinose.en_US
dc.format.extent344289 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleThe chemical synthesis of 2-keto-3-deoxy-octonate and its cleavage by a specific aldolaseen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelNatural Resources and Environmenten_US
dc.subject.hlbsecondlevelMolecular, Cellular and Developmental Biologyen_US
dc.subject.hlbsecondlevelEcology and Evolutionary Biologyen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Bacteriology, The University of Michigan, Ann Arbor, USA; Rackham Arthritis Research Unit, The University of Michigan, Ann Arbor, USAen_US
dc.contributor.affiliationumDepartment of Bacteriology, The University of Michigan, Ann Arbor, USA ; Rackham Arthritis Research Unit, The University of Michigan, Ann Arbor, USAen_US
dc.identifier.pmid13960611en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/32223/1/0000283.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0006-291X(63)90559-Xen_US
dc.identifier.sourceBiochemical and Biophysical Research Communicationsen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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