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Autor:
C.A. Martinwixtrom, R.W. Estabrook, Manjunath S. Shet, C.W. Fisher, Y. Saeki, M.P. Arlotto, C.H.L. Shackleton, P.L. Holmans
Publikováno v:
Archives of Biochemistry and Biophysics. 311:402-417
A fusion protein containing the heme domain of bovine cytochrome P450 17A and the flavin domains of rat NADPH-cytochrome P450 reductase has been genetically engineered by linking the modified cDNAs for each gene with the codons for serine and threoni
Publikováno v:
Archives of biochemistry and biophysics. 318(2)
The recombinant fusion protein containing the heme domain of human P450 3A4 and the flavin domains of rat NADPH-cytochrome P450 (P450) reductase (rF450[mHum3A4/mRat0R]L1) requires both phospholipid and detergent as well as cytochrome b 5 (b 5 ) for t
Publikováno v:
Archives of biochemistry and biophysics. 312(2)
A T7 expression system is described for the high-level production in Escherichia coli of the membrane-bound form of human and rat cytochrome b5. The cDNAs of b5 have been engineered to contain a coding sequence for a four-member histidine domain at t
Autor:
E. Simpson, R.W. Estabrook
Publikováno v:
Advances in Enzyme Regulation. 7:259-279
Studies on the distribution of malic enzyme in bovine adrenal cortex have shown that this tissue contains two forms of the enzyme, one in the cytosol, and the other in the mitochondria. The mitochondrial malic enzyme activity has been shown to be a s
Publikováno v:
Scopus-Elsevier
The regiospecificity of arachidonic acid oxygenation, catalyzed by rat liver microsomal fractions in the presence of NADPH, can be altered by animal pretreatment with a fibric acid type of hypolipidemic drug, ciprofibrate. While microsomal fractions
Autor:
A.A. Akhrem, L.M. Alexander, A.P. Alvares, B.N. Ames, T. Aralso, A.I. Archakov, E Arinç, R.N. Armstrong, M.J. Arnaud, E. Bachmann, L. Balk, L.M. Ball, J. Baron, L.S. Baskin, N. Beaty, P.M. Belanger, G.D. Bellward, P. Bentley, F.E. Beyhl, R.C. Blake, H. Bonkowsky, A.R. Boobis, B. Bösterling, G.S. Boyd, E. Bresnick, J.W. Bridges, J.A. Bumpus, C. Chen, Y.L. Chlang, A.K. Cho, S.K. Clinton, G. Cohen, A.H. Conney, M.W. Coomes, M.J. Coon, M.A. Correia, C.J. Coscla, P.M. Dansette, J.H. Dees, M. Delaforge, F.A. de la Iglesia, T.R. Devereux, R.N. Dubois, H.B. Dunford, P.H. Duquette, F. Durst, R.E. Ebel, E. Elsenstadt, L. Ernster, R.W. Estabrook, W.E. Fahl, G.C. Farrell, G. Feuer, R. Feyereisen, M.R. Franklin, R.B. Franklin, J.S. French, T.G. Geary, H.V. Gelboin, G.G. Gibson, J.R. Gillette, H.R. Glatt, I.B. Glowinski, D.M. Goldberg, J.W. Gorrod, E.M. Gozukara, H. Graf, C.J. Grandjean, B.W. Griffin, J.T. Groves, F.P. Guengerich, I.C. Gunsalus, J.-Å. Gustafsson, J.R. Halpert, B.D. Hammock, O. Hankinson, O. Hänninen, R.P. Hanzlik, O. Hayaishi, C. Heidelberger, G. Heinemeyer, E. Hietanen, A.G. Hildebrandt, R.N. Hines, M.J. Hintz, P. Hlavica, E. Hodgson, J. Högberg, J.L. Holtzman, J.P. Horwitz, L. Hulett, D.E. Hultquist, R.M. Hyslop, K. Ichlhara, Y. Ichlkawa, M. Ingeiman-Sundberg, T. lyanagl, J. Jansson, E.H. Jeffery, D.M. Jerina, B. Jernström, E.F. Johnson, T. Kamataki, L.S. Kaminsky, J. Kapituinik, F.C. Kauffman, J.C. Kawalek, S. Kawano, G.L. Kedderis, S.R. Keyes, T. Kimura, D.R. Koop, D. Kupfer, B.N. La Du, J.D. Lambeth, F.C.P. Law, M.C. Lechner, S.S. Lee, W. Legrum, W. Lenk, W. Levin, C.S. Leiber, S.L. Longacre, I.S. Longmulr, A.Y.H. Lu, P. Lundberg, V. Luu-The, M.G. Macdonald, P.N. Magee, G.J. Mannering, B. Mannervlk, B.S.S. Masters, T. Matsushlma, D.R. Mattison, P. Maurel, G.D. McCoy, U.A. Meyer, J.J. Mieyal, G.T. Miwa, P. Moldèus, J. Montelius, A. Morello, R. Morgenstern, M.J. Murphy, R.I. Murray, A. Nadezhdin, S. Narasimhulu, R.A. Neal, D.W. Nebert, M. Neglshi, S. Nigam, R.L. Norman, R.F. Novak, P.J. O'Brien, F. Oesch, R.T. Okita, K. Okuda, C.J. Omiecinski, T. Omura, D.D. Oprian, N.R. Orme-Johnson, S. Orrenius, P.R. Ortiz de Montellano, Y. Osawa, G. Padmanaban, M.W. Pariza, S.S. Pawar, F.J. Peterson, J.A. Peterson, R.M. Philpot, J.L. Plummer, L.R. Pohl, R.J. Pohl, C.F. Polnaszek, G. Powis, R.A. Prough, A.D. Rahimtula, D.J. Reed, L.A. Reinke, S.A. Rice, I. Roots, K. Ruckpaul, H.H. Ruf, D.E. Ryan, J. Rydström, S. Safe, R. Sato, J.B. Schenkman, J. Seldegård, I.R. Senciall, H.G. Shertzer, Z.H. Siddik, P. Sinclair, S.R. Slaughter, S.G. Sligar, B.R. Smith, S.J. Stohs, H.W. Strobel, G.D. Sweeney, R. Talcott, H. Tanlguchl, P.E. Thomas, H. Thor, S.S. Thorgeirsson, R.G. Thurman, R. Toftgård, A. Tunek, V. Ullrich, T.A. van der Hoeven, M.E. van Liar, K.P. Vatsls, J.L. Vermilion, M. Vore, C. Welborn, J. Werringloer, S.B. West, R.A. White, R.E. White, R.A. Wiley, E.D. Wills, C.R. Wolf, T. Yamano, C.S. Yang, S.K. Yang, Y. Yasukochi, K.T. Yasunobu, A. Yawetz, Y. Yoshlda, A. Yuasa, V.G. Zannoni, D.M. Ziegler
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8ddc7598241b7e79630af1716406a88d
https://doi.org/10.1016/b978-0-12-187701-9.50003-6
https://doi.org/10.1016/b978-0-12-187701-9.50003-6
Publisher Summary This chapter discusses thermal measurements during oxidative reactions, and describes the design and operating characteristics of a differential calorimeter suitable for measurement of enthalpy changes during metabolism by fragile s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5ca7e1704887c5b20cc3dc02187dd335
https://doi.org/10.1016/0076-6879(67)10118-3
https://doi.org/10.1016/0076-6879(67)10118-3