Purification and characterization of a microsomal cytochrome P-450 IIB enzyme from sheep lung

References

• Ainc E. Characterization of sheep liver and lung microsomal ethylmorphine N-demethylase. Comparative Biochemistry and Physiology 1985; 80B: 389–399
   Google Scholar
• Arinc E., Iscan M. Y. Comparative studies of sheep liver and lung microsomal aniline 4-hydroxylase. Comparative Biochemistry and Physiology 1983; 74C: 151–158
   Google Scholar
• Bend J. R., Serabjit-Singh C. J., Philpot R. M. The pulmonary uptake, accumulation, and metabolism of xenobiotics. Annual Review of Toxicology 1985; 25: 97–127
   PubMed Web of Science ®Google Scholar
• Burnette W. N. ‘Western blotting’: electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Analytical Biochemistry 1981; 112: 195–203
   PubMed Web of Science ®Google Scholar
• Cochin J., Axelrod J. Biochemical and pharmacological changes in the rat following chronic administration of morphine, nalorphine and normorphine. Journal of Pharmacology and Experimental Therapeutics 1959; 125: 105–110
   PubMed Web of Science ®Google Scholar
• De Pierre J. W., Moron M. S., Johannesen K. A. M., Ernster L. A reliable, sensitive, and convenient radioactive assay for benzpyrene monooxygenase. Analytical Biochemistry 1975; 63: 470–484
   PubMed Web of Science ®Google Scholar
• Duignan D. B., Sipes I. G., Leonard T. B., Halpert J. R. Purification and characterization of the dog hepatic cytochrome P-459 isozyme responsible for the metabolism of 2,2′,4,4′, 5,5′-hexachlorobiphenyl. Archives of Biochemistry and Biophysics 1987; 255: 290–303
   PubMed Web of Science ®Google Scholar
• Estabrook R. W., Peterson J., Baron J., Hildebrant A. The spectrophotometric measurement of turbid suspensions of cytochromes associated with drug metabolism. Methods in Pharmacology 1972; 2: 303–305
   Google Scholar
• Fujii-Kuriyama Y., Mizukami Y., Kawajiri K., Sogawa K., Muramatsu M. Primary structure of a cytochrome P-450: coding nucleotide sequence of phenobarbital-inducible cytochrome P-450 cDNA from rat liver. Proceedings of the National Academy of Sciences, USA 1982; 79: 2793–2797
   PubMed Web of Science ®Google Scholar
• Fujita V. S., Black S. D., Tarr G. E., Koop D. R., Coon M. J. On the amino acid sequence of cytochrome P-450 isozyme 4 from rabbit liver microsomes. Proceedings of the National Academy of Sciences, USA 1984; 81: 4260–4264
   PubMed Web of Science ®Google Scholar
• Gasser R., Philpot R. M. Primary structures of cytochrome P-450 isozyme 5 from rabbit and rat and regulation of species-dependent expression and induction in lung and liver: identification of cytochrome P-450 gene subfamily IVB. Molecular Pharmacology 1989; 35: 617–625
   PubMed Web of Science ®Google Scholar
• Gonzalez F. J. The molecular biology of cytochrome P-450s. Pharmacological Reviews 1989; 40: 243–288
   Web of Science ®Google Scholar
• Gram T. E., Sikic B. I., Litterst C. L., Mimnaugh E. G., Drew R., Siddik Z. H. The role of the lung in the metabolism and disposition of xenobiotics, in Industrial and Environmental Xenobiotics: in vitro versus in vivo. Biotransformation and Toxicity, J. R. Fouts, I. Gut. Excerpta Medica, Amsterdam 1978; 53–58
   Google Scholar
• Guengerich F. P. Preparation and properties of highly purified cytochrome P-450 and NADPH-cytochrome P-450 reductase from pulmonary microsomes of untreated rabbits. Molecular Pharmacology 1977; 13: 911–923
   PubMed Web of Science ®Google Scholar
• Guengerich F. P. Purification and characterization of xenobiotic-metabolizing enzymes from lung tissue. Pharmacology and Therapeutics 1990; 45: 299–307
   PubMed Web of Science ®Google Scholar
• Hugli T. E., Moore S. Determination of the tryptophan content of proteins by ion exchange chromatography of alkaline hydrolysates. Journal of Biological Chemistry 1972; 247: 2828–2834
   PubMed Web of Science ®Google Scholar
• Iscan M. Y., Arinc E. Kinetic and structural properties of biocatalytically active sheep lung microsomal N ADPH-cytochrome c reductase. International Journal of Biochemistry 1986; 18: 731–741
   PubMedGoogle Scholar
• Iscan M. Y., Arinc E. Comparison of highly purified sheep liver and lung NADPH-cytochrome P-450 reductases by the analysis of kinetic and catalytic properties. International Journal of Biochemistry 1988; 20: 1189–1196
   PubMedGoogle Scholar
• Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680–685
   PubMed Web of Science ®Google Scholar
• Larrieu G., Galtier P. A comparative study of some oxidative and conjugative drug metabolizing enzymes in liver, lung and kidney of sheep. Comparative Biochemistry and Physiology 1988; 89C: 225–228
   Google Scholar
• Lowry O. H., Rosebrough N. J., Farr A. L., Randall R. J. Protein measurement with the Folin phenol Teagent. Journal of Biological Chemistry 1951; 193: 265–275
   PubMed Web of Science ®Google Scholar
• Masters B. S. S., Muerhoff A. S., Okita R. T. Enzymology of extrahepatic cytochrome P-450. Mammalian Cytochromes P-450, F. P. Guengerich. CRC Press, Boca Raton, FL 1987; 107–137
   Google Scholar
• Minchin R. F., Boyd M. R. Localization of metabolic activation and deactivation systems in the lung: significance to the pulmonary toxicity of xenobiotics. Annual Review of Pharmacology and Toxicology 1983; 23: 217–238
   PubMed Web of Science ®Google Scholar
• Nebert D. W., Gonzalez F. J. P450 genes: structure, evolution, and regulation. Annual Review of Biochemistry 1987; 56: 943–993
   Web of Science ®Google Scholar
• Ozols J., Heinemann F. S., Johnson E. F. The complete amino acid sequence of a constitutive form of liver microsomal cytochrome P-450. Journal of Biological Chemistry 1985; 260: 5427–5434
   PubMed Web of Science ®Google Scholar
• Parandoosh Z., Fujita V. S., Coon M. J., Philpot R. M. Cytochrome P-450 isozymes 2 and 5 in rabbit lung and liver. Comparisons of structure and inducibility. Drug Metabolism and Disposition 1987; 15: 59–67
   PubMed Web of Science ®Google Scholar
• Philpot R. M., Smith B. R. Role of cytochrome P-450 and related enzymes in the pulmonary metabolism of xenobiotics. Environmental Health Perspectives 1984; 55: 359–367
   PubMed Web of Science ®Google Scholar
• Serabjit-Singh C. J., Wolf C. R., Philpot R. M. The rabbit pulmonary-monooxygenase system. Immunochemical and biochemical characterization of enzyme components. Journal of Biological Chemistry 1979; 254: 9901–9907
   PubMed Web of Science ®Google Scholar
• Serabjit-Singh C. J., Albro P. W., Robertson I. G. C., Philpot R. M. Interactions between xenobiotics that increase or decrease the levels of cytochrome P-450 isozymes in rabbit lung and liver. Journal of Biological Chemistry 1983; 258: 12827–12834
   PubMed Web of Science ®Google Scholar
• Shigenaga M. K., Trevor A. J., Castagnoli N., Jr. Metabolism-dependent covalent binding of (S)-[5-3H]nicotine to liver and lung microsomal macromolecules. Drug Metabolism and Disposition 1988; 16: 397–402
   PubMed Web of Science ®Google Scholar
• Tarr G. E., Black S. D., Fujita V. S., Coon M. J. Complete amino acid sequence and predicted membrane topology of phenobarbital-induced cytochrome P-450 (isozyme 2) from rabbit liver microsomes. Proceedings of the National Academy of Sciences, USA 1983; 80: 6552–6556
   PubMed Web of Science ®Google Scholar
• Williams D. E., Hale S. E., Okita R. T., Masters B. S. S. A prostaglandin ω-hydroxylase cytochrome P-450 (P-450PG-ω) purified from lungs of pregnant rabbits. Journal of Biological Chemistry 1984; 259: 14600–14608
   PubMed Web of Science ®Google Scholar
• Williams D. E., Meyer H. H., Dutchuk M. S. Distinct pulmonary and hepatic forms of flavin-containing monooxygenase in sheep. Comparative Biochemistry and Physiology 1989; 93B: 465–470
   Google Scholar
• Williams D. E., Shigenaga M. K., Castagnoli N., Jr. The role of cytochromes P-450 and flavin-containing monooxygenase in the metabolism of (S)-nicotine by rabbit lung. Drug Metabolism and Disposition 1990; 18: 418–428
   PubMed Web of Science ®Google Scholar
• Yang C. S., Tu Y. Y., Koop D. R., Coon M. J. Metabolism of nitrosamines by purified rabbit liver cytochrome P-450 isozymes. Cancer Research 1985; 45: 1140–1145
   PubMed Web of Science ®Google Scholar
• Yasukochi Y., Masters B. S. S. Some properties of a detergent-solubilized NADPH-cytochrome c (cytochrome P-450) reductase purified by biospecific affinity chromatography. Journal of Biological Chemistry 1976; 251: 5337–5344
   PubMed Web of Science ®Google Scholar
• Yost G. S., Buckpitt A. R., Roth R. A., McLemore T. L. Mechanisms of lung injury by systemically administered chemicals. Toxicology and Applied Pharmacology 1989; 101: 179–195
   PubMed Web of Science ®Google Scholar