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Purification and characterization of cytochrome P450 2E2 from hepatic microsomes of neonatal rabbits

dc.contributor.authorDing, Xinxinen_US
dc.contributor.authorPernecky, Steven J.en_US
dc.contributor.authorCoon, Minor J.en_US
dc.date.accessioned2006-04-10T14:29:42Z
dc.date.available2006-04-10T14:29:42Z
dc.date.issued1991-12en_US
dc.identifier.citationDing, Xinxin, Pernecky, Steven J., Coon, Minor J. (1991/12)."Purification and characterization of cytochrome P450 2E2 from hepatic microsomes of neonatal rabbits." Archives of Biochemistry and Biophysics 291(2): 270-276. <http://hdl.handle.net/2027.42/29002>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6WB5-4DN9YBB-122/2/3ac344dbefd79caf0f44e2801b27f158en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/29002
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=1952940&dopt=citationen_US
dc.description.abstractThe alcohol-inducible P450 2E subfamily in the rabbit has two known members that differ in only 16 amino acid residues scattered throughout the polypeptide chain. P450 2E1 has been thoroughly characterized, and is known to have diverse inducers and substrates. Little is known, however, about the properties of P450 2E2, since efforts to isolate this isozyme from adult rabbits have been unsuccessful. In the present study, 2E2 was purified to electrophoretic homogeneity from liver microsomes of neonatal rabbits with the use of 4-methylpyrazole as a stabilizing agent. The purified cytochrome was identified as 2E2 by NH2-terminal amino acid sequence analysis as well as by immunoblot analysis with three different antibodies to 2E1. Purified 2E2, in contrast to 2E1, is predominantly low-spin in the presence of 20% glycerol, but is in a mixed high- and low-spin state as the concentration of glycerol is decreased. The catalytic properties of purified 2E1 and 2E2 were compared in the reconstituted system with a variety of substrates, including alcohols, ethers nitrosamines, and aromatic compounds. Differences between the two enzymes in catalytic activity and in the interaction with cytochrome b5 were observed with some but not all of the substrates tested. Purified 2E1 and 2E2 both consume molecular oxygen relatively rapidly during NADPH oxidation in the absence of an added substrate, and stoichiometric determinations indicated that only about 20% of the O2 was reduced to H2O2, with the remainder apparently undergoing four-electron reduction to water.en_US
dc.format.extent2024934 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titlePurification and characterization of cytochrome P450 2E2 from hepatic microsomes of neonatal rabbitsen_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, Medical School, The University of Michigan, Ann Arbor, Michigan 48109-0606, USAen_US
dc.contributor.affiliationumDepartment of Biological Chemistry, Medical School, The University of Michigan, Ann Arbor, Michigan 48109-0606, USAen_US
dc.contributor.affiliationumDepartment of Biological Chemistry, Medical School, The University of Michigan, Ann Arbor, Michigan 48109-0606, USAen_US
dc.identifier.pmid1952940en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/29002/1/0000031.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0003-9861(91)90134-5en_US
dc.identifier.sourceArchives of Biochemistry and Biophysicsen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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