Cytochrome P-450 purified to apparent homogeneity from phenobarbital-induced rabbit liver microsomes: Catalytic activity and other properties
dc.contributor.author | van der Hoeven, Theodore A. | en_US |
dc.contributor.author | Haugen, David A. | en_US |
dc.contributor.author | Coon, Minor J. | en_US |
dc.date.accessioned | 2006-04-07T16:44:08Z | |
dc.date.available | 2006-04-07T16:44:08Z | |
dc.date.issued | 1974-09-23 | en_US |
dc.identifier.citation | van der Hoeven, Theodore A., Haugen, David A., Coon, Minor J. (1974/09/23)."Cytochrome P-450 purified to apparent homogeneity from phenobarbital-induced rabbit liver microsomes: Catalytic activity and other properties." Biochemical and Biophysical Research Communications 60(2): 569-575. <http://hdl.handle.net/2027.42/22272> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6WBK-4DNB473-11N/2/02b332bf89c441fd2291bcb1ad109140 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/22272 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=4418358&dopt=citation | en_US |
dc.description.abstract | Cytochrome P-450 was purified to a content of over 17 nmoles per mg of protein from liver microsomes of phenobarbital-treated rabbits by fractionation with polyethylene glycol 6000, DEAE-cellulose column chromatography, and hydroxylapatite column chromatography in the presence of Renex 690, a nonionic detergent. The purified preparation exhibited a single polypeptide band (molecular weight, 49,000 daltons) when submitted to SDS-polyacrylamide gel electrophoresis. Cytochromes P-420 and 5 and NADPH-cytochrome reductase were absent. The reconstituted system containing purified cytochrome P-450, reductase, and phosphatidylcholine catalyzed the hydroxylation of benzphetamine, cyclohexane, aniline, and laurate. | en_US |
dc.format.extent | 594597 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Cytochrome P-450 purified to apparent homogeneity from phenobarbital-induced rabbit liver microsomes: Catalytic activity and other properties | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Natural Resources and Environment | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbsecondlevel | Ecology and Evolutionary Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry Medical School, The University of Michigan, Ann Arbor, Michigan 48104, USA | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry Medical School, The University of Michigan, Ann Arbor, Michigan 48104, USA | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry Medical School, The University of Michigan, Ann Arbor, Michigan 48104, USA | en_US |
dc.identifier.pmid | 4418358 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/22272/1/0000711.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0006-291X(74)90278-2 | en_US |
dc.identifier.source | Biochemical and Biophysical Research Communications | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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