Rabbit, cytochrome

Once the resolution has been optimized as a function of gradient rate, one can continue to fine-tune the separation, raising flow rate and temperature. In a study of temperature and flowrate variation on the separation of the tryptic peptides from rabbit cytochrome c, column performance doubled while analysis time was reduced by almost half using this strategy.97 Commercially available software has been developed to aid in optimization. As a final note, in an industrial laboratory optimization is not completed until a separation has been shown to be rugged. It is a common experience to optimize a separation on one column, only to find that separation fails on a second column of identical type. Reproducibility and rigorous quality control in column manufacture remains a goal to be attained. 

Guengerich, F.P., Krauser, (.A. and Johnson, W.W. (2004) Rate-limiting steps in oxidations catalyzed by rabbit cytochrome P450 1A2. Biochemistry, 43 (10), 775. 

Johnson EF, Schwab GE, Vickery LE. Positive effectors of the binding of an active site-directed amino steroid to rabbit cytochrome P-450 3c. J Biol Chem 1988 263 (33) 17672-17677. 

Yamamoto Y, Ishizuka M, Takada A, et al. Cloning, tissue distribution, and functional expression of two novel rabbit cytochrome P450 isozymes, CYP2D23 and CYP2D24. J Biochem 1998 124 503-508. 

A stock solution of rabbit Cytochrome c was made up in water at a concentration of 4.3 mg/ml. The concentration of the stock solution was determined by quantitative amino acid analysis of a 5pJ aliquot that was hydrolyzed and analyzed as previously described (4). The stock solution was diluted 5-fold with 0. IM ammonium bicarbonate or 0. IM sodium borate (both at pH 8.2) and TPCK-Trypsin in lOmM HCl was added to give a 1 20 enzyme protein solution (w/w). Digestion was carried out at 37°C for 24 hours after which the enzymatic activity was terminated by heating at 100°C for 5 min. 

Trudell JR, Bosterling B, Trevor AJ. Reductive metabolism of halothane by human and rabbit cytochrome P-450. Binding of 1 -chloro-2,2,2-trifluoroethyl radical to phospholipids. Mol Pharmacol 1982 21(3) 710-7. 

Shou, M., Korzekwa, K. R., Crespi, C. L., Gonzalez, F. J., and Gelboin, H. V. (1994) The role of 12 cDNA-expressed human, rodent, and rabbit cytochrome P450 in the metabolism of benzo[a]pyrene and benzo[a]pyrene trans-7,8-dihydrodiol. Mol. Carcinog. 10 (3), 159-68. 

Miller, G.P. and F.P. Guengerieh (2001). Binding and oxidation of alkyl 4-nitrophenyl ethers by rabbit cytochrome P450 1A2 Evidence for two binding sites. Biochemistry 40, 7262-7272. 

N.G. Rainov, and C.M. Kramm (2002). Differential cytotoxicity and bystander effect of the rabbit cytochrome P450 4B1 enzyme gene by two different prodrugs Implications for pharma-cogene therapy. Cancer Gene Ther. 9, 178-188. 

Expression of rabbit cytochrome P4504A which catalyzes the oo-hydroxylation of fatty acids, and prostaglandins. Arch. Biochem. Biophys. 307, 57-67. 

Shah MB, Wilderman PR, Pascual J, Zhang Q, Stout CD, Halpert JR (2012) Conformational adaptation of human cytochrome P450 2B6 and rabbit cytochrome P450 2B4 revealed upon binding multiple amlodipine molecules. Biochemistry 51 7225 7238... 

Pernecky SJ, Porter TD, Coon MJ (1990) Expression of rabbit cytochrome P-450IIE2 in yeast and stabilization of the enzyme by 4-methylpyrazole. Biochem Biophys Res Commun 172 1331-1337... 

Laethem RM, Koop DR (1992) (Iden)tification of rabbit cytochromes P450 2C1 and 2C2 as arachidonic acid epoxygenases. Mol Pharmacol 42 958-963... 

Oae and coworkers oxidized several diaryl, dialkyl and alkyl aryl sulfides to their corresponding sulfoxides using purified cytochrome P-450 obtained from rabbit liver microsomes138. In agreement with expectations, this enzyme did not exhibit much stereospecificity. Some examples including the observed e.e. values are shown by 121-125. A model was proposed to account for the absolute configurations of the sulfoxides produced (126). The sulfur atom is preferentially oxidized from the direction indicated. 

The oxidation of a series of cyclic and acyclic sulphides by cytochrome P 450from rabbit liver gave sulphoxides with / -configuration at sulphur. The maximum of the e.e. value (53.8%) was observed for benzyl t-butyl sulphoxide310. 

A more detailed study of the biological oxidation of sulphoxides to sulphones has been reported165. In this study cytochrome P-450 was obtained in a purified form from rabbit cells and was found to promote the oxidation of a series of sulphoxides to sulphones by NADPH and oxygen (equation 56). Kinetic measurements showed that the process proceeds by a one-electron transfer to the activated enzymatic intermediate [an oxenoid represented by (FeO)3+] according to equation (57). 

Relatively few human studies that address the metabolism of alkyl lead compounds were found in the available literature. The dealkylation, mediated by cytochrome P-450, of alkyl lead compounds is thought to occur in the rat, mouse, and rabbit. This step converts tetraethyl and tetramethyl lead to the... 

Cytochrome P450 2E1, rabbit Hairy root Atropa belladonna A. rhizogenes transformation of leaf explant CaMV 35S Not reported Not reported 22... 

O Donnell et al. [70] found that LOX and not cyclooxygenase, cytochrome P-450, NO synthase, NADPH oxidase, xanthine oxidase, ribonucleotide reductase, or mitochondrial respiratory chain is responsible for TNF-a-mediated apoptosis of murine fibrosarcoma cells. 15-LOX activity was found to increase sharply in heart, lung, and vascular tissues of rabbits by hypercholesterolemia [71], Schnurr et al. [72] demonstrated that there is an inverse regulation of 12/15-LOXs and phospholipid hydroperoxide glutathione peroxidases in cells, which balanced the intracellular concentration of oxidized lipids. 

Sawamura A, Kusunose E, Satouchi K, et al. Catalytic properties of rabbit kidney fatty acid omega-hydroxylase cytochrome P-450ka2 (CYP4A7). Biochim Biophys Acta 1993 1168(1 ) 30-36. 

Mathews JM, Bend JR. N-alkylaminobenzotriazoles as isozyme-selective suicide inhibitors of rabbit pulmonary microsomal cytochrome P-450. Mol Pharmacol 1986 30(l) 25-32. 

Kocarek, T.A., Schuetz, E.G., Strom, S.C., Fisher, R.A. and Guzelian, P.S. (1995) Comparative analysis of cytochrome P4503A induction in primary cultures of rat, rabbit, and human hepatocytes. 

Curiously this parallels the discovery of MC inducible cytochrome P-1+50 in fetal and neonatal rabbits (1+3) which, a) fails to... 

Atlas, S.A., Boobis, A.R., Felton, J.S., Thorgeirsson, S.S. and Hebert, D.W. Ontogenetic expression of polycyclic aromatic compound-inducible monooxygenase activities and forms of cytochrome P-1+50 in rabbit. J. Biol. Chem. (1977) 252, 1+712-1+721. 

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