Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1978 Jun 15;172(3):479–486. doi: 10.1042/bj1720479

Liver enzyme induction by 1,1,1-trichloro-2,2-bis-(p-chlorophenyl)ethane (DDT) is accompanied by an increase in the specific activity of elongation factor 1.

E T Young, D M Nicholls
PMCID: PMC1185721  PMID: 249658

Abstract

Homogenates of liver were obtained from control rats and from rats that had received DDT [1,1,1-trichloro-2,2-bis(p-chlorophenyl)ethane]. The postmicrosomal supernatant fractions were used for the purification of elongation factor 1 by hydroxyapatite chromatography and phosphocellulose chromarography. The amount of binding factor present was essentially the same for both groups of animals, but the specific activity, as measured by the binding assay, was about twice as high in the DDT-treated preparations. After sucrose-gradient sedimentation, the difference in specific activity was found to reside in the low-molecular-weight (50000) form of elongation factor 1. The implications of an increased reactivity of elongation factor 1 during the induction of membrane enzymes are discussed.

Full text

PDF
479

Images in this article

485Fig. 4.
on p.485

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Arias I. M., Doyle D., Schimke R. T. Studies on the synthesis and degradation of proteins of the endoplasmic reticulum of rat liver. J Biol Chem. 1969 Jun 25;244(12):3303–3315. [PubMed] [Google Scholar]
  2. Bolla R., Brot N. Age dependent changes in enzymes involved in macromolecular synthesis in Turbatrix aceti. Arch Biochem Biophys. 1975 Jul;169(1):227–236. doi: 10.1016/0003-9861(75)90336-7. [DOI] [PubMed] [Google Scholar]
  3. Bolla R., Weissbach H., Brot N. Multiple forms of elongation factor 1 in various rat tissues. Arch Biochem Biophys. 1975 Feb;166(2):683–684. doi: 10.1016/0003-9861(75)90433-6. [DOI] [PubMed] [Google Scholar]
  4. Bunyan P. J., Townsend M. G., Taylor A. Pesticide-induced changes in hepatic microsomal enzyme systems. Some effects of 1,1-DI(p-chlorophenyl)-2,2,2-trichloroethane (DDT) and 1,1-DI(p-chlorophenyl)-2,2-dichloroethylene (DDE) in the rat and Japanese quail. Chem Biol Interact. 1972 Jun;5(1):13–26. doi: 10.1016/0009-2797(72)90043-9. [DOI] [PubMed] [Google Scholar]
  5. Cappon I. D., Nicholis D. M. Factors involved in increased protein synthesis in rat kidney after administration of DDT. Chem Biol Interact. 1974 Dec;9(6):395–409. doi: 10.1016/0009-2797(74)90021-0. [DOI] [PubMed] [Google Scholar]
  6. Cappon I. D., Nicholls D. M. DDT increases the aminoacyl-tRNA binding activity of liver pH 5 supernatant fraction. Chem Biol Interact. 1974 Sep;9(3):155–168. doi: 10.1016/s0009-2797(74)80001-3. [DOI] [PubMed] [Google Scholar]
  7. Cappon I. D., Young E. T., Nicholls D. M. An environmental chemical, polychlorinated biphenyl, increases the protein synthesizing activity of liver and kidney pH 5 supernatant fractions. Chem Biol Interact. 1976 Jul;14(1-2):127–134. doi: 10.1016/0009-2797(76)90030-2. [DOI] [PubMed] [Google Scholar]
  8. Chan Y. P., Sendecki W., Nicholls D. M. Effect of 7,12-dimethylbenz(a)anthracene on the binding of aminoacyl transfer RNA in rat liver. Cancer Res. 1977 Nov;37(11):4220–4227. [PubMed] [Google Scholar]
  9. Collins J. F., Moon H. M., Maxwell E. S. Multiple forms and some properties of aminoacyltransferase I (elongation factor I) from rat liver. Biochemistry. 1972 Oct 24;11(22):4187–4194. doi: 10.1021/bi00772a024. [DOI] [PubMed] [Google Scholar]
  10. Dehlinger P. J., Schimke R. T. Effects of phenobarbital, 3-methylcholanthrene, and hematin on the synthesis of protein components of rat liver microsomal membranes. J Biol Chem. 1972 Feb 25;247(4):1257–1264. [PubMed] [Google Scholar]
  11. Drews J., Bednarik K., Grasmuk H. Elongation factor 1 from Krebs II mouse ascites cells. Purification, structure and enzymatic properties. Eur J Biochem. 1974 Jan 16;41(2):217–227. doi: 10.1111/j.1432-1033.1974.tb03263.x. [DOI] [PubMed] [Google Scholar]
  12. GASIOR E., MOLDAVE K. RESOLUTION OF AMINOACYL-TRANSFERRING ENZYMES FROM RAT LIVER BY MOLECULAR SIEVE CHROMATOGRAPHY. J Biol Chem. 1965 Aug;240:3346–3352. [PubMed] [Google Scholar]
  13. GELBOIN H. V., BLACKBURN N. R. THE STIMULATORY EFFECT OF 3-METHYLCHOLANTHRENE ON BENZPYRENE HYDROXYLASE ACTIVITY IN SEVERAL RAT TISSUES: INHIBITION BY ACTINOMYCIN D AND PUROMYCIN. Cancer Res. 1964 Feb;24:356–360. [PubMed] [Google Scholar]
  14. Gielen J. E., Nebert D. W. Aryl hydrocarbon hydroxylase induction in mammalian liver cell culture. I. Stimulation of enzyme activity in nonhepatic cells and in hepatic cells by phenobarbital, polycyclic hydrocarbons, and 2,2-bis(p-chlorophenyl)-1,1,1-trichloroethane. J Biol Chem. 1971 Sep 10;246(17):5189–5198. [PubMed] [Google Scholar]
  15. Girgis G. R., Nicholls D. M. Control of the increased protein synthesis in kidney of nephrotic rats by supernatant factors. Biochim Biophys Acta. 1971 Oct 14;247(2):335–347. doi: 10.1016/0005-2787(71)90681-2. [DOI] [PubMed] [Google Scholar]
  16. Girgis G. R., Nicholls D. M. Protein synthesis limited by transferase I. Biochim Biophys Acta. 1972 May 29;269(3):465–476. doi: 10.1016/0005-2787(72)90134-7. [DOI] [PubMed] [Google Scholar]
  17. Grasmuk H., Nolan R. D., Drews J. Functional identity of the monomeric and multiple forms of elongation-factor 1 from Krebs-II mouse ascites-tumor cells. Eur J Biochem. 1976 Aug 16;67(2):421–431. doi: 10.1111/j.1432-1033.1976.tb10707.x. [DOI] [PubMed] [Google Scholar]
  18. Iwasaki K., Mizumoto K., Tanaka M., Kaziro Y. A new protein factor required for polypeptide elongation in mammalian tissues. J Biochem. 1973 Oct;74(4):849–852. doi: 10.1093/oxfordjournals.jbchem.a130311. [DOI] [PubMed] [Google Scholar]
  19. Kotsiopoulos P. S., Mohr S. C. Protein synthesis elongation factor 1 from rat liver: a zinc metalloenzyme. Biochem Biophys Res Commun. 1975 Dec 1;67(3):979–987. doi: 10.1016/0006-291x(75)90771-8. [DOI] [PubMed] [Google Scholar]
  20. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  21. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  22. Lanzani G. A., Giannattasio M., Manzocchi L. A., Bollini R., Soffientini A. N., Macchia V. The influence of cyclic GMP on polypeptide synthesis in a cell-free system derived from wheat embryos. Biochem Biophys Res Commun. 1974 May 7;58(1):172–177. doi: 10.1016/0006-291x(74)90907-3. [DOI] [PubMed] [Google Scholar]
  23. Malkin M., Lipmann F. Fusidic acid: inhibition of factor T2 in reticulocyte protein synthesis. Science. 1969 Apr 4;164(3875):71–72. doi: 10.1126/science.164.3875.71. [DOI] [PubMed] [Google Scholar]
  24. McEwen Nicholls D., Carey J., Sendecki W. Growth of liver accompanied by an increased binding of aminoacyl-transfer ribonucleic acids. Biochem J. 1977 Sep 15;166(3):463–471. doi: 10.1042/bj1660463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. McEwen D., Ng K. Regeneration of renal proximal tubules after mercuric chloride injury is accompanied by increased binding of aminoacyl-transfer ribonucleic acid. Biochem J. 1976 Nov 15;160(2):357–365. doi: 10.1042/bj1600357. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Moon H. M., Redfield B., Millard S., Vane F., Weissbach H. Multiple forms of elongation factor 1 from calf brain. Proc Natl Acad Sci U S A. 1973 Dec;70(12):3282–3286. doi: 10.1073/pnas.70.12.3282. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Nagata S., Iwasaki K., Kaziro Y. Distribution of the low molecular weight form of eukaryotic elongation factor 1 in various tissues. J Biochem. 1976 Jul;80(1):73–77. doi: 10.1093/oxfordjournals.jbchem.a131260. [DOI] [PubMed] [Google Scholar]
  28. Nicholls D. M., Chan Y. P., Girgis G. R. Aminoacyl-tRNA binding activity in regenerating kidney following contralateral nephrectomy or administration of folic acid. Dev Biol. 1975 Nov;47(1):1–11. doi: 10.1016/0012-1606(75)90259-6. [DOI] [PubMed] [Google Scholar]
  29. Nicholls D. M., Petryshyn R., Warner L. Laser irradiation induces increased activity of liver elongation factor 1. Radiat Res. 1974 Oct;60(1):98–107. [PubMed] [Google Scholar]
  30. Nombela C., Redfield B., Ochoa S., Weissbach H. Elongation factor 1 from Artemia salina: properties and disaggregation of the enzyme. Eur J Biochem. 1976 Jun 1;65(2):395–402. doi: 10.1111/j.1432-1033.1976.tb10353.x. [DOI] [PubMed] [Google Scholar]
  31. O'Farrell P. H. High resolution two-dimensional electrophoresis of proteins. J Biol Chem. 1975 May 25;250(10):4007–4021. [PMC free article] [PubMed] [Google Scholar]
  32. Petryshyn R. A., Creasy R. C., Nicholls D. M. Protein synthesis in the heart of genetic dystrophic mice. Biochem Med. 1977 Oct;18(2):139–151. doi: 10.1016/0006-2944(77)90085-0. [DOI] [PubMed] [Google Scholar]
  33. Platt D. S., Cockrill B. L. Biochemical changes in rat liver in response to treatment with drugs and other agents. II. Effects of halothane, DDT, other chlorinated hydrocarbons, thioacetamide, dimethylnitrosamine and ethionine. Biochem Pharmacol. 1969 Feb;18(2):445–457. doi: 10.1016/0006-2952(69)90221-4. [DOI] [PubMed] [Google Scholar]
  34. Prather N., Ravel J. M., Hardesty B., Shive W. Evidence for activities of rabbit reticulocyte elongation factor 1 analogous to bacterial factors EF-Ts and EF-Tu. Biochem Biophys Res Commun. 1974 Apr 8;57(3):578–583. doi: 10.1016/0006-291x(74)90585-3. [DOI] [PubMed] [Google Scholar]
  35. Raeburn S., Collins J. F., Moon H. M., Maxwell E. S. Aminoacyltransferase II from rat liver. I. Purification and enzymatic properties. J Biol Chem. 1971 Feb 25;246(4):1041–1048. [PubMed] [Google Scholar]
  36. Schneir M., Moldave K. The isolation and biological activity of multiple forms of aminoacyl transferase I of rat liver. Biochim Biophys Acta. 1968 Aug 23;166(1):58–67. doi: 10.1016/0005-2787(68)90490-5. [DOI] [PubMed] [Google Scholar]
  37. Slobin L. I., Möller W. Changes in form of elongation factor during development of Artemia salina. Nature. 1975 Dec 4;258(5534):452–454. doi: 10.1038/258452a0. [DOI] [PubMed] [Google Scholar]
  38. Studier F. W. Analysis of bacteriophage T7 early RNAs and proteins on slab gels. J Mol Biol. 1973 Sep 15;79(2):237–248. doi: 10.1016/0022-2836(73)90003-x. [DOI] [PubMed] [Google Scholar]
  39. TOMBS M. P., SOUTER F., MACLAGAN N. F. The spectrophotometric determination of protein at 210 millimicrons. Biochem J. 1959 Sep;73:167–171. doi: 10.1042/bj0730167. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Tarragó A., Allende J. E., Redfield B., Weissbach H. The effect of guanosine nucleotides on the multiple forms of protein synthesis elongation factor 1 from wheat embryos. Arch Biochem Biophys. 1973 Nov;159(1):353–361. doi: 10.1016/0003-9861(73)90461-x. [DOI] [PubMed] [Google Scholar]
  41. Twardowski T., Hill J. M., Weissbach H. Studies on the disaggregation of EF-1 with carboxypeptidase A. Arch Biochem Biophys. 1977 Apr 30;180(2):444–451. doi: 10.1016/0003-9861(77)90058-3. [DOI] [PubMed] [Google Scholar]
  42. Twardowski T., Legocki A. B. Purification and some properties of elongation factor 2 from wheat germ. Biochim Biophys Acta. 1973 Sep 28;324(1):171–183. doi: 10.1016/0005-2787(73)90261-x. [DOI] [PubMed] [Google Scholar]
  43. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]
  44. Weissbach H., Ochoa S. Soluble factors required for eukaryotic protein synthesis. Annu Rev Biochem. 1976;45:191–216. doi: 10.1146/annurev.bi.45.070176.001203. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES