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Expression of rabbit cytochrome P-450IIE2 in yeast and stabilization of the enzyme by 4-methylpyrazole

dc.contributor.authorPernecky, Steven J.en_US
dc.contributor.authorPorter, Todd D.en_US
dc.contributor.authorCoon, Minor J.en_US
dc.date.accessioned2006-04-10T13:33:39Z
dc.date.available2006-04-10T13:33:39Z
dc.date.issued1990-11-15en_US
dc.identifier.citationPernecky, Steven J., Porter, Todd D., Coon, Minor J. (1990/11/15)."Expression of rabbit cytochrome P-450IIE2 in yeast and stabilization of the enzyme by 4-methylpyrazole." Biochemical and Biophysical Research Communications 172(3): 1331-1337. <http://hdl.handle.net/2027.42/28310>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6WBK-4F030CK-5D/2/ac73898c55efc7b35ae9c35eaf9d3025en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/28310
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=2173920&dopt=citationen_US
dc.description.abstractA rabbit cytochrome P-450IIE2 full-length cDNA was cloned into a yeast episomal plasmid (YEp13) between the copper-responsive yeast metallothionein gene promoter (CUP1) and the iso-1-cytochrome c gene terminator (CYC1), and the cytochrome P-450 was expressed in Saccharomyces cerevisiae. The microsomal fraction prepared from copper-treated cells exhibited a ferrous carbonyl difference spectrum with an absorption maximum at 451 nm and contained approximately 0.07 nmol of P-450IIE2 per mg of protein. The P-450IIE2 protein expressed in yeast microsomes was catalytically competent as judged by the NADPH-dependent deethylation of N-nitrosodiethylamine and by the oxidation of butanol. Cholate solubilization and polyethylene glycol fractionation of yeast microsomal P-450IIE2 yielded a preparation with a markedly lower specific content than that of intact microsomes, but, when 4-methylpyrazole was included during solubilization, the holoenzyme was completely stabilized.en_US
dc.format.extent569762 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleExpression of rabbit cytochrome P-450IIE2 in yeast and stabilization of the enzyme by 4-methylpyrazoleen_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, Medical School, The University of Michigan, Ann Arbor, MI 48109, USAen_US
dc.contributor.affiliationumDepartment of Biological Chemistry, Medical School, The University of Michigan, Ann Arbor, MI 48109, USAen_US
dc.contributor.affiliationumDepartment of Biological Chemistry, Medical School, The University of Michigan, Ann Arbor, MI 48109, USAen_US
dc.identifier.pmid2173920en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/28310/1/0000066.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0006-291X(90)91595-Jen_US
dc.identifier.sourceBiochemical and Biophysical Research Communicationsen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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