Role of a hydrophobic polypeptide in the N-terminal region of NADPH-cytochrome P-450 reductase in complex formation with P-450
dc.contributor.author | Black, Shaun D. | en_US |
dc.contributor.author | French, John S. | en_US |
dc.contributor.author | Williams, Charles H., Jr. | en_US |
dc.contributor.author | Coon, Minor J. | en_US |
dc.date.accessioned | 2006-04-07T17:30:53Z | |
dc.date.available | 2006-04-07T17:30:53Z | |
dc.date.issued | 1979-12-28 | en_US |
dc.identifier.citation | Black, Shaun D., French, John S., Williams, Jr., Charles H., Coon, Minor J. (1979/12/28)."Role of a hydrophobic polypeptide in the N-terminal region of NADPH-cytochrome P-450 reductase in complex formation with P-450." Biochemical and Biophysical Research Communications 91(4): 1528-1535. <http://hdl.handle.net/2027.42/23437> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6WBK-4DMXD5H-1X8/2/897ca905c153815b09ca853f2b604e4d | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/23437 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=118758&dopt=citation | en_US |
dc.description.abstract | Detergent-solubilized liver microsomal NADPH-cytochrome P-450 reductase is known to retain the ability to catalyze electron transfer to cytochrome P-450, whereas the trypsin-solubilized reductase does not. In the present study, treatment of the highly purified detergent-solubilized rabbit liver enzyme (m.w. 77,700) with trypsin was shown to yield a small peptide (m.w. 6,100) as well as the large peptide (m.w. 71,200) which retains the flavin prosthetic groups. The small peptide, which is hydrophobic in nature as shown by its amino acid composition and solubility properties, is apparently the moiety in the native reductase involved in binding to cytochrome P-450 and to the microsomal membrane. The C-terminal amino acid sequences of the native reductase and large fragment are identical [-Trp-(Leu, Val)-Asp-Ser-COOH], thereby indicating that the hydrophobic peptide is located in the N-terminal region of the enzyme. | en_US |
dc.format.extent | 703802 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 | Role of a hydrophobic polypeptide in the N-terminal region of NADPH-cytochrome P-450 reductase in complex formation with P-450 | 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 | Veterans Administration Medical Center, Ann Arbor, Michigan 48109, USA; Department of Biological Chemistry Medical School, The University of Michigan, Ann Arbor, Michigan 48109, USA | en_US |
dc.contributor.affiliationum | Veterans Administration Medical Center, Ann Arbor, Michigan 48109, USA; Department of Biological Chemistry Medical School, The University of Michigan, Ann Arbor, Michigan 48109, USA | en_US |
dc.contributor.affiliationum | Veterans Administration Medical Center, Ann Arbor, Michigan 48109, USA; Department of Biological Chemistry Medical School, The University of Michigan, Ann Arbor, Michigan 48109, USA | en_US |
dc.contributor.affiliationum | Veterans Administration Medical Center, Ann Arbor, Michigan 48109, USA; Department of Biological Chemistry Medical School, The University of Michigan, Ann Arbor, Michigan 48109, USA | en_US |
dc.identifier.pmid | 118758 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/23437/1/0000385.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0006-291X(79)91238-5 | en_US |
dc.identifier.source | Biochemical and Biophysical Research Communications | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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