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Alcohol oxidation by isozyme 3a of liver microsomal cytochrome P-450
dc.contributor.authorCoon, Minor J.en_US
dc.contributor.authorKoop, Dennis R.en_US
dc.contributor.authorMorgan, Edward T.en_US
dc.date.accessioned2006-04-07T18:48:37Z
dc.date.available2006-04-07T18:48:37Z
dc.date.issued1983en_US
dc.identifier.citationCoon, Minor J., Koop, Dennis R., Morgan, Edward T. (1983)."Alcohol oxidation by isozyme 3a of liver microsomal cytochrome P-450." Pharmacology Biochemistry and Behavior 18(Supplement 1): 177-180. <http://hdl.handle.net/2027.42/25379>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6T0N-477XRK2-116/2/cb1b547fd9caa21c229f38b1c227f708en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/25379
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6685296&dopt=citationen_US
dc.description.abstractLiver microsomes from rabbits treated chronically with ethanol were solubilized and fractionated to yield a new isozyme of cytochrome P-450 in a homogeneous state. This cytochrome, designated as isozyme 3a on the basis of its relative electrophoretic mobility, is distinct from the known isozymes as judged by its spectral properties, minimal molecular weight, amino acid composition, and NH2- and COOH-terminal amino acid sequences. In addition, peptide mapping by high performance liquid chromatography following trypsinolysis indicates that form 3a is a unique gene product. This cytochrome has unusually high activity in the oxidation of ethanol and other alcohols to aldehydes and in the p-hydroxylation of aniline as compared with the other isozymes of P-450. The ethanol-oxidizing activity of isozyme 3a, which requires the presence of NADPH and NADPH-cytochrome P-450 reductase and is stimulated by the presence of phosphatidylcholine, is not due to contamination by catalase or an NAD+-or NADP+-dependent alcohol dehydrogenase.en_US
dc.format.extent405170 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleAlcohol oxidation by isozyme 3a of liver microsomal cytochrome P-450en_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelBiological Chemistryen_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, 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.pmid6685296en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/25379/1/0000828.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0091-3057(83)90168-5en_US
dc.identifier.sourcePharmacology Biochemistry and Behavioren_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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