Use of monoclonal antibody probes against rat hepatic cytochromes P-450c and P-450d to detect immunochemically related isozymes in liver microsomes from different species
dc.contributor.author | Thomas, Paul E. | en_US |
dc.contributor.author | Reidy, Judith | en_US |
dc.contributor.author | Reik, Linda M. | en_US |
dc.contributor.author | Ryan, Dene E. | en_US |
dc.contributor.author | Koop, Dennis R. | en_US |
dc.contributor.author | Levin, Wayne | en_US |
dc.date.accessioned | 2006-04-07T18:17:32Z | |
dc.date.available | 2006-04-07T18:17:32Z | |
dc.date.issued | 1984-11-15 | en_US |
dc.identifier.citation | Thomas, Paul E., Reidy, Judith, Reik, Linda M., Ryan, Dene E., Koop, Dennis R., Levin, Wayne (1984/11/15)."Use of monoclonal antibody probes against rat hepatic cytochromes P-450c and P-450d to detect immunochemically related isozymes in liver microsomes from different species." Archives of Biochemistry and Biophysics 235(1): 239-253. <http://hdl.handle.net/2027.42/24640> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6WB5-4DN9STY-61/2/5c560dea15f8dadf43c3cb931b34df64 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/24640 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6208847&dopt=citation | en_US |
dc.description.abstract | Nine distinct monoclonal antibodies raised against purified rat liver cytochrome P-450c react with six different epitopes on the antigen, and one of these epitopes is shared by cytochrome P-450d. None of these monoclonal antibodies recognize seven other purified rat liver isozymes (cytochromes P-450a, b, and e-i) or other proteins in the cytochrome P-450 region of "Western blots" of liver microsomes. Each of the monoclonal antibodies was used to probe "Western blots" of liver microsomes from untreated, or 3-methylcholanthrene-, or isosafrole-treated animals to determine if laboratory animals other than rats possess isozymes immunochemically related to cytochromes P-450 and P-450d. Two protein-staining bands immunorelated to cytochromes P-450c and P-450d were observed in all animals treated with 3-methylcholanthrene (rabbit, hamster, guinea pig, and C57BL/6J mouse) except the DBA/2J mouse, where no polypeptide immunorelated to cytochrome P-450c was detected. The conservation of the number of rat cytochrome P-450c epitopes among these species varied from as few as two (guinea pig) to as many as five epitopes (C57BL/6J mouse and rabbit). The relative mobility in sodium dodecyl sulfate-gels of polypeptides immunorelated to cytochromes P-450c and P-450d was similar in all species examined except the guinea pig, where the polypeptide related to cytochrome P-450c had a smaller Mr than cytochrome P-450d. With the use of both monoclonal and polyclonal antibodies, we were able to establish that purified rabbit cytochromes P-450 LM4 and P-450 LM6 are immunorelated to rat cytochromes P-450d and P-450c, respectively. | en_US |
dc.format.extent | 6703947 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 | Use of monoclonal antibody probes against rat hepatic cytochromes P-450c and P-450d to detect immunochemically related isozymes in liver microsomes from different species | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Public Health | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbsecondlevel | Biological Chemistry | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Health Sciences | 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 48109, U.S.A. | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, Medical School, The University of Michigan, Ann Arbor, Michigan 48109, U.S.A. | en_US |
dc.contributor.affiliationother | Department of Experimental Carcinogenesis and Metabolism, Hoffmann-La Roche Inc., Nutley, New Jersey 07110, U.S.A | en_US |
dc.contributor.affiliationother | Department of Experimental Carcinogenesis and Metabolism, Hoffmann-La Roche Inc., Nutley, New Jersey 07110, U.S.A | en_US |
dc.contributor.affiliationother | Department of Experimental Carcinogenesis and Metabolism, Hoffmann-La Roche Inc., Nutley, New Jersey 07110, U.S.A | en_US |
dc.contributor.affiliationother | Department of Experimental Carcinogenesis and Metabolism, Hoffmann-La Roche Inc., Nutley, New Jersey 07110, U.S.A | en_US |
dc.identifier.pmid | 6208847 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/24640/1/0000051.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0003-9861(84)90273-X | en_US |
dc.identifier.source | Archives of Biochemistry and Biophysics | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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