Summary
Measurement of the effect of drugs on the in vivo rates of synthesis of rabbit liver organelle bound proteins were measured following individual treatments with the inducers phenobarbital, 3-methylcholanthrene and PCB (a mixture of polychlorinated biphenyls) and the inhibitors, cycloheximide, aflatoxin 13, chloramphenicol and actinomycin D. Following their isolation from a homogenate containing the combined livers of 14C-leucine injected experimental animals and 3H-leucine injected control animals, purified fractions of the following proteins were prepared: microsomal cytochrome b5, cytochrome P-450, NADH-cytochrome b5 reductase, NADPH-cytochrome P-450 reductase and proteolipids, outer mitochrondrial membrane cytochrome b5, NADH-cytochrome b5 reductase and proteolipids, inner mitochrondrial membrane cytochrome c, NADH dehydrogenase and proteolipids, intermitochrondrial membrane cytochrome b5 and circulating serum albumin.
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References
Kuntzman, R. 1969. Ann. Rev. Pharmacol. 9, 21–27.
Kuriama, T., Omura, T., Siekevitz, P. and Palade, G. E. 1969. J. Biol. Chem. 244, 2017–2026.
Arias, I. M., Doyle, D. and Schimke, R. T. 1969. J. Biol. Chem. 244, 3303–3315.
Dehlinger, P. J. and Schimke, R. T. 1972. J. Biol. Chem. 247, 1257–1264.
Raw, I. 1978. Fed. Proc., 37, 1544.
Schenkman, J. B. and Centi, D. L. 1978. Methods in Enzymology (Colowick S. P. and Kaplan N. O.), ed. 52, 83–89, Academic Press, N.Y.
Fukushima, K. and Sato, R. 1973. Biochem. J. (Tokyo), 74,161–173.
Raw, I. 1978. Biochem. Biophys. Res. Commun. 81, 1294–1297.
Ozols, J. 1974. Biochemistry 13, 426–433.
Hara, T. and Minakami, S. 1970. J. Biochem. (Tokyo) 67,741–743.
Fujita, T., Showman, D. W. & Mannering, G. J. 1973. J. Biol. Chem. 248, 2192–2201.
Imai, Y., and Sato, R. 1974. Biochem. Biophys. Res. Commun. 60, 8–14.
Yasukochi, Y. and Masters, B.S.S. 1976. J. Biol. Chem. 254,5337–5343.
Gozales-Cadavid, N. F. and Campbell, P. N. 1967. Biochem. J. 105, 427–441.
Cohen, H. J. and Fridovich, I. 1971. J. Biol. Chem. 246,359–366.
Folch-Pi, J. and Stoffyn, P. 1972. Ann. N.Y. Acad. Sci. 195,86–107.
Tzagoloff, A., Akai, A. 1972. J. Biol. Chem. 247, 6517–6523.
Stoffyn, P. and Folch-Pi, J. 1971. Biochem. Biophys. Res. Commun. 44, 154–161.
Howe, P. E. 1921. J. Biol. Chem. 49, 109–113.
Omura, T. and Sato, R. 1964. J. Biol. Chem. 239, 2379–2385.
Stripp, B., Hamrick, M. E., and Gillete, J. R. 1972. Biochem. Pharmacol. 21, 747–751.
Matern, S., Frohling, W. and Bock, K. W. 1974. Nauhyn-Schmiedebergs Arch. Pharmacol. 273, 242–247.
Matsumura, A. and Omura, T. 1973. J. Biochem. (Tokyo), 73, 407–416.
Dryan, R., DeBernard, B. and Rabinovitz, M. 1969. J. biol. Chem. 244, 5874–5878.
Raw, I. and Mahler, H. R. 1959. J. Biol. Chem. 234, 1867–1873.
Sottocasa, G. L. Kuylenstierna, B., Ernster, L. and Bergstrand, A. 1967. J. Cell Biol., 32, 415–438.
Coon, M. J., van der Howven, T. Z., Dahl, S. B. and Haugen, D. A. 1978. Methods in Enzymology (Colowick S. P. and Kaplan N. O.), 52, 109–117, Academic Press, N.Y.
Haugen, D. A., Coon, M. J. and Nebert D. W. 1976, J. Biol. Chem., 251, 1817–1827.
Shichi, H., Sugimura, Y. and Funahashi, S. 1964. Biochem. Biophys. Acta, 97, 483–291.
Shichi, H. Sugimura, Y. and Funahashi, S. 1964. biochem, Biophys. Acta, 97, 492–297.
Cattell, K. J., Lindop, C. R., Knight, I. G. and Beechey, R. B. 1971. Biochem. J. 125, 169–177.
Racker, E. and Eytan, E. 1977. J. Biol. Chem., 250, 7533–7534.
Farber, J. L. and Farmar, R. 1973. Biochem. Biophys. Res. commun. 51, 626–630.
Kahl, G. F., Kahl, R., Kumari, K. and Neubert, D. W. 1976. J. Biol. Chem. 251, 5397–5407.
Rothblum, L. I., Devlin, T. M. and Ch'hi, J. J. 1976. Biochem. J. 156, 151–157.
Ch'hi, J. J., Procyk, R. and Devlin, T. M. 1977. Biochem. J. 162, 501–507.
Ernest, M. J., DeLap, L. and Feigelson, P. 1978. J. Biol. Chem. 253, 2895–2897.
Levine, J. H., Nicholson, W. E. and Orth, D. N. 1975. Proc. Nat. Acad. Sci. USA, 72, 2279–2283.
Patterson, D. S. P. 1973. Food Cosmet. Toxicol. 11, 287–293.
Sidransky, H., Verney, E. Murty, C. N., Sarma, D. S. R. and Reid, M. 1977. Chem-Biol. Interactions 18, 69–82.
Reid, I. M., Sarma, S. S. R., and Sidransky, H. 1971. Lab Invest. 25, 141–148.
Murty, C. N. and Sidransky, H. 1972. Biochem. Biophys. Acta 281, 69–78.
John, D. W. and Miller, L. L. 1966. J. Biol. Chem. 241, 4817–4824.
Wilson, S. H., Hill, H. Z. and Hoagland, M. B. 1967. Biochem. J. 103, 567–572.
Tagaki, M. and Ogata, K. 1968. Biochem. Biophys. Res. Commun., 33, 55–61.
Gonzales-Cadavid, N., Orga, J. P. and Gonzales, M., 1971. Biochem. J., 124, 685–694.
Firkin, F. C., and Linnane, A. W. 1969. Exp. Cell Res. 55,68–76.
Hallman, M. 1971. Biochem. Pharmacol. 20, 1797–1809.
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This research was supported by grants from the PSC-BHE Research Award Program of The City University of New York, US Public Health Service Grant SO 7 PRO7132-07 and the Alma Toorock Fund for Cancer Research.
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Raw, I., Rockwell, P. Effect of a single dose of inducers and inhibitors on the rate of synthesis of cytochromes and reductases in liver organelles. Mol Cell Biochem 28, 7–16 (1979). https://doi.org/10.1007/BF00223355
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DOI: https://doi.org/10.1007/BF00223355