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Membrane topology of microsomal cytochrome P-450: Saturation transfer EPR and freeze-fracture electron microscopy studies

dc.contributor.authorSchwarz, D.en_US
dc.contributor.authorPirrwitz, J.en_US
dc.contributor.authorMeyer, H. W.en_US
dc.contributor.authorCoon, M. J.en_US
dc.contributor.authorRuckpaul, K.en_US
dc.date.accessioned2006-04-10T13:38:06Z
dc.date.available2006-04-10T13:38:06Z
dc.date.issued1990-08-31en_US
dc.identifier.citationSchwarz, D., Pirrwitz, J., Meyer, H. W., Coon, M. J., Ruckpaul, K. (1990/08/31)."Membrane topology of microsomal cytochrome P-450: Saturation transfer EPR and freeze-fracture electron microscopy studies." Biochemical and Biophysical Research Communications 171(1): 175-181. <http://hdl.handle.net/2027.42/28421>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6WBK-4DP5MDD-1S/2/45268c7651a86400bf6f519e258067a1en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/28421
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=2168169&dopt=citationen_US
dc.description.abstractThe rotation of cytochrome P-450 LM2 (CYPIIB4) incorporated into large microsomal-like lipid vesicles was investigated by saturation transfer EPR using 15N- and 2H-substituted spin labels. In combination with rotational diffusion, the distribution and size of protein particles in the bilayer were studied by freeze-fracture electron microscopy. The data from both methods suggest an oligomeric and membrane-spanning aggregate for the topology of microsomal cytochrome P-450.en_US
dc.format.extent2701979 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleMembrane topology of microsomal cytochrome P-450: Saturation transfer EPR and freeze-fracture electron microscopy studiesen_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.affiliationumThe University of Michigan, Ann Arbor, Michigan, USAen_US
dc.contributor.affiliationotherCentral Institute for Molecular Biology, Academy of Sciences of GDR, 1115, Berlin-Buch, GDRen_US
dc.contributor.affiliationotherDeutsches Wollforschungsinstitut, Aachen, FRGen_US
dc.contributor.affiliationotherFriedrich Schiller University, Jena, GDRen_US
dc.contributor.affiliationotherCentral Institute for Molecular Biology, Academy of Sciences of GDR, 1115, Berlin-Buch, GDRen_US
dc.identifier.pmid2168169en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/28421/1/0000204.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0006-291X(90)91373-Zen_US
dc.identifier.sourceBiochemical and Biophysical Research Communicationsen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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