Highly purified detergent-solubilized NADPH-cytochrome P-450 reductase from phenobarbital-induced rat liver microsomes
dc.contributor.author | Vermilion, Janice L. | en_US |
dc.contributor.author | Coon, Minor J. | en_US |
dc.date.accessioned | 2006-04-07T16:43:30Z | |
dc.date.available | 2006-04-07T16:43:30Z | |
dc.date.issued | 1974-10-23 | en_US |
dc.identifier.citation | Vermilion, Janice L., Coon, Minor J. (1974/10/23)."Highly purified detergent-solubilized NADPH-cytochrome P-450 reductase from phenobarbital-induced rat liver microsomes." Biochemical and Biophysical Research Communications 60(4): 1315-1322. <http://hdl.handle.net/2027.42/22251> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6WBK-4F02W3B-B1/2/723e3f655b79df5805a1dabb5bc0a016 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/22251 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=4153862&dopt=citation | en_US |
dc.description.abstract | NADPH-cytochrome P-450 reductase was highly purified from liver microsomes of phenobarbital-induced rats by column chromatography on DEAE-cellulose, DEAE-Sephadex A-50, and hydroxylapatite in the presence of deoxycholate or Renex 690, a nonionic detergent. The purified enzyme gave a single major band with a molecular weight of 79,000 daltons on SDS-polyacrylamide gel electrophoresis. FMN and FAD were present in about equal amounts. The most active reductase preparation catalyzed the reduction of 40.9 [mu]moles of cytochrome per min per mg of protein and, as an indirect measure of cytochrome P-450 reduction, the oxidation of 2.0 [mu]moles of NADPH per min per mg of protein in a reconstituted hydroxylation system containing benzphetamine as the substrate. | en_US |
dc.format.extent | 562486 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 | Highly purified detergent-solubilized NADPH-cytochrome P-450 reductase from phenobarbital-induced rat liver microsomes | 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.identifier.pmid | 4153862 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/22251/1/0000687.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0006-291X(74)90341-6 | en_US |
dc.identifier.source | Biochemical and Biophysical Research Communications | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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