Page 246 - The Toxicology of Fishes
P. 246

226                                                        The Toxicology of Fishes


                       Larsen, H. E., Celander, M., and Goksøyr, A., The cytochrome-p450 system of Atlantic salmon (Salmo salar).
                          2. Variations in hepatic catalytic activities and isozyme patterns during an annual reproductive-cycle, Fish
                          Physiol. Biochem., 10, 291, 1992.
                       Leaver M. J. and George, S. G., A piscine glutathione S-transferase which efficiently conjugates the end-
                          products of lipid peroxidation, Mar. Environ. Res., 46, 71, 1998.
                       Leaver, M. J. and George, S. G., A cytochrome P4501B gene from a fish, Pleuronectes platessa, Gene, 256,
                          83, 2000.
                       Leaver, M. J., Clarke, D. J., and George, S. G., Molecular studies of the phase II xenobiotic conjugative
                          enzymes of marine Pleuronectid flatfish, Aquatic. Toxicol., 22, 265, 1992.
                       Leaver, M. J., Scott, K., and George, S. G., Cloning and characterisation of the major hepatic glutathione
                          S-transferase from a marine teleost flatfish, the plaice (Pleuronectes platessa) with structural similarities
                          to plant, insect and mammalian theta class isoenzymes, Biochem. J., 292, 189, 1993.
                       Leaver, M. J., Wright, J., and George, S. G., Structure and expression of a cluster of glutathione S-transferase
                          genes from a marine fish, the plaice (Pleuronectes platessa), Biochem. J., 321, 405, 1997.
                       Leaver,M. J., Wright, J., Hodgson, P., Boukouvala, E., and George, S. G., Piscine UDP-glucuronosyltransferase
                          1B. Aquat. Toxicol., 84, 356–365, 2007.
                       Lech, J. J. and Costrini, N. V., In vitro and in vivo metabolism of 3-trifluoromethyl-4-nitrophenol (TFM) in
                          rainbow trout, Comp. Gen. Pharmacol., 3, 160, 1972.
                       Lee, S. J. and Buhler, D. R., Functional properties of a rainbow trout CYP3A27 expressed by recombinant
                          baculovirus in insect cells, Drug Metab. Disp., 30, 1406, 2002.
                       Lee, S. J. and Buhler, D. R., Cloning, tissue distribution, and functional studies of a new cytochrome P450
                          3A subfamily member, CYP3A45, from rainbow trout (Oncorhynchus mykiss) intestinal ceca,  Arch.
                          Biochem. Biophys., 412, 77, 2003.
                       Lee, S. J. et al., Cloning, sequencing, and tissue expression of CYP3A27, a new member of the CYP3A
                          subfamily from embryonic and adult rainbow trout livers, Arch. Biochem. Biophys., 360, 53, 1998.
                       Lee, S. J. et al., Immunohistochemical localization and differential expression of cytochrome P450 3A27 in
                          the gastrointestinal tract of rainbow trout, Toxicol. Appl. Pharmacol., 177, 94, 2001.
                       Lemaire, P. et al., Stimulation of oxyradical production of hepatic microsomes of flounder (Platichthys flesus)
                          and perch (Perca fluviatilis) by model and pollutant xenobiotics, Arch. Environ. Cont. Toxicol., 26, 191,
                          1994.
                       Lemaire, P., Forlin, L., and Livingstone, D. R., Responses of hepatic biotransformation and antioxidant
                          enzymes to CYP1A-inducers (3-methylcholanthrene, β-naphthoflavone) in sea bass (Dicentrarchus la-
                          brax), dab (Limanda limanda), and rainbow trout (Oncorhynchus mykiss), Aquat. Toxicol., 36, 141, 1996.
                       Lesca, P. et al., Structure–activity relationships in the inhibitory effects of ellipticines on benzo(a)pyrene
                          hydroxylase activity and 3-methylcholanthrene mutagenicity, Biochem. Pharmacol., 29, 3231, 1980.
                       Levi, P. E. and Hodgson, E., Metabolism of organophosphorus compounds by the flavin-containing monoox-
                          ygenase, in  Organophosphates: Chemistry,  Fate and Effects, Chambers, J. E. and Levi, P. E., Eds.,
                          Academic Press, San Diego, CA, 1992, pp. 141–154.
                       Levine, S. L., Czosnyka, H., and Oris, J. T., Effect of the fungicide clotrimazole on the bioconcentration of
                          benzo[a]pyrene in gizzard shad (Dorosoma cepedianum): in vivo and in vitro inhibition of cytochrome
                          P4501A activity, Environ. Toxicol. Chem., 16, 306, 1997.
                       Li, A. P., Kaminski, D. L., and Rasmussen, A., Substrates of human hepatic cytochrome P450 3A4, Toxicol.
                          Appl. Pharmacol., 15, 1, 1995.
                       Li, Y. and Jaiswal, A. K., Regulation of human NAD(P)H:quinone oxidoreductase gene: role of AP1 binding
                          site contained within human antioxidant response element, J. Biol. Chem. 267, 15097, 1992 (erratum in
                          J. Biol. Chem., 268, 21454, 1993).
                       Liehr, J. G. and Ricci, M. J., 4-Hydroxylation of estrogens as a marker of human mammary tumors, Proc.
                          Natl. Acad. Sci. U.S.A., 93, 3294, 1996.
                       Little, P. J. et al., Imidazole derivatives as inhibitors of cytochrome P450-dependent oxidation and activators
                          of epoxide hydrolase in hepatic microsomes from a marine fish, Biochem. Pharmacol., 30, 2876, 1981.
                       Lotlikar, P. D. et al., Modulation of microsome-mediated aflatoxin B 1  binding to exogenous and endogenous
                          DNA by cytosolic glutathione S-transferases in rat and hamster livers, Carcinogenesis, 5, 269, 1984.
                       Loveland, P. M. et al., Formation of aflatoxin B 1  from aflatoxicol by rainbow trout (Salmo Gairdneri) liver
                          in vitro, Res. Commun. Chem. Pathol. Pharmacol., 16, 167, 1977.
   241   242   243   244   245   246   247   248   249   250   251