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Polymorphism in fowl serum albumin. VI. Changes in in vitro protein synthesizing activity in developing embryonic fowl liver

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Cell-free protein synthesizing systems were prepared from the livers of chick embryos at selected ages and the characteristics of individual fractions were compared. While polysomes showed decreasing size with older embryos, isolated polysomes did not differ significantly in amino acid incorporating activity when assayed with standard cell sap. When assayed with standard polysomes, cell sap activity decreased with increasing developmental age whether incorporation was measured using [3H]lysine, [3H]leucine, or [3H]aminoacyl-tRNA. Free amino acid concentrations in the cell sap showed reproducible independent variation during development which was taken into consideration in calculating net amino acid incorporation. A large increase in ribonuclease activity was observed during development; however, nuclease inhibitor activity was absent before day 15 but increased thereafter. Aminoacyl-tRNA synthetase activity did not vary significantly. It is proposed that the observed changes in the rate of cell-free protein synthesis result not only from increasing ribonuclease activity with increasing developmental age but also from changes in the activity of other soluble factors.

This is paper VI in a series; paper V is reference 6. The series title is based on earlier work with systems derived from fowl which synthesized two genetic variants of serum albumin21.

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References

  1. Campbell, P. N. and Kernot, B. A. 1959. Biochem. J. 72, 6P.

  2. Siler, J. G. and Fried, M. 1968. Biochem. J. 109, 185–190.

    Google Scholar 

  3. Zimmerman, D. H. and Fried, M. 1971. Comp. Biochem. Physiol. 38B, 239–245.

    Google Scholar 

  4. Jernigan, H. M., Iacona, M. A. and Fried, M. 1972. Biochim. Biophys. Acta 287, 538–547.

    Google Scholar 

  5. Jernigan, H. M., Chu, M. and Fried, M. 1973. Biochim. Biophys. Acta 312, 502–508.

    Google Scholar 

  6. Jernigan, H. M., LaMonda, G. W. and Fried, M. 1976. Comp. Biochem. Physiol. 53B, 67–72.

    Google Scholar 

  7. Chu, M. H., Jernigan, H. M., and Fried, M. 1978. Biochim. Biophys. Acta, 518, 298–307.

    Google Scholar 

  8. Pain, V. M. 1973. Biochim. Biophys. Acta, 308, 180–187.

    Google Scholar 

  9. Von Ehrenstein, G. 1967. Meth. Enzymol. 12A, 588–596.

    Google Scholar 

  10. Stulberg, M. P. and Novelli, G. D. 1962. Enzymol. 5, 703–707.

    Google Scholar 

  11. Anfinsen, C. B., Redfield, R. R., Choate, W. L., Page, J. and Carroll, W. R. 1954. J. Biol. Chem. 207, 201–210.

    Google Scholar 

  12. Utsinomiya, T. and Roth, J. S. 1966. J. Cell Biol. 29, 395–403.

    Google Scholar 

  13. Roth, J. S. 1956. Biochim. Biophys. Acta 21, 34–43.

    Google Scholar 

  14. Gilbert, J. M. and Anderson, W. F. 1970. J. Biol. Chem. 245, 2342–2349.

    Google Scholar 

  15. Hampel, A. and Enger, M. D. 1973. J. Mol. Biol. 79, 285–293.

    Google Scholar 

  16. Roth, J. S. 1962. Biochim. Biophys. Acta 61, 903–915.

    Google Scholar 

  17. Shortman, K. 1962. Biochim. Biophys. Acta 61, 50–55.

    Google Scholar 

  18. Arora, D. J. S. and de Lamirande, G. 1967. Can. J. Biochem. 45, 1021–1026.

    Google Scholar 

  19. Moriyama, T., Umedia, T., Nakashima, S., Oura, H. and Tsukada, J. 1969. J. Biochem. 66, 151–156.

    Google Scholar 

  20. Sheppard, E. P., Hogan, K. and Roberts, K. B. 1970. Biochim. Biophys. Acta 217, 159–163.

    Google Scholar 

  21. Fried, M. and Chun, P. W. 1971. Comp. Biochem. Physiol. 39B, 523–540.

    Google Scholar 

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This research was supported in part by a grant from the Damon Runyon Memorial Fund (DRG-1125). Dr. H. M. Jernigan was an N.I.H. Postdoctoral Fellow (5 F02 GM 50944-02).

To whom all inquiries are to be addressed.

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Chu, ML.H., Jernigan, H.M., Iacona, M.A. et al. Polymorphism in fowl serum albumin. VI. Changes in in vitro protein synthesizing activity in developing embryonic fowl liver. Mol Cell Biochem 24, 167–174 (1979). https://doi.org/10.1007/BF00220735

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