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Effects of nitroaromatic compounds on spectra of D-amino acid oxidase
dc.contributor.authorNishino, Tomokoen_US
dc.contributor.authorNishino, Takeshien_US
dc.contributor.authorMassey, Vincenten_US
dc.date.accessioned2006-04-07T17:23:18Z
dc.date.available2006-04-07T17:23:18Z
dc.date.issued1980-07-16en_US
dc.identifier.citationNishino, Tomoko, Nishino, Takeshi, Massey, Vincent (1980/07/16)."Effects of nitroaromatic compounds on spectra of D-amino acid oxidase." Biochemical and Biophysical Research Communications 95(1): 312-319. <http://hdl.handle.net/2027.42/23199>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6WBK-4DN95M1-10F/2/ebdf26fbb1b574066db3fb027eb6f1been_US
dc.identifier.urihttps://hdl.handle.net/2027.42/23199
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6106474&dopt=citationen_US
dc.description.abstractD-amino acid oxidase (D-amino acid oxygen oxidoreductase E.C. 1.4.3.3.) was found to bind various nitroaromatics with characteristic spectral changes similar in form to those caused by benzoate and its analogues. Nitrobenzene and o-nitroaniline were found to be competitive inhibitors of the enzyme. Dissociation constants of nitroaromatics tested were larger than those of the carboxylates except in the case of o-nitroaniline. Dinitrophenol was also found to bind to the enzyme with almost the same value of dissociation constant as nitrobenzene; on the other hand, dicarboxylates had no complex ability (3).en_US
dc.format.extent422435 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleEffects of nitroaromatic compounds on spectra of D-amino acid oxidaseen_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 Biological Chemistry, University of Michigan, Ann Arbor, Michigan, 48109, U.S.A.en_US
dc.contributor.affiliationotherDepartment of Biochemistry, Yokohama City University School of Medicine, Minami-ku, Yokohama, Japan 232.en_US
dc.contributor.affiliationotherDepartment of Biochemistry, Yokohama City University School of Medicine, Minami-ku, Yokohama, Japan 232.en_US
dc.identifier.pmid6106474en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/23199/1/0000126.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0006-291X(80)90740-8en_US
dc.identifier.sourceBiochemical and Biophysical Research Communicationsen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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