Molecular and Cellular Biochemistry

, Volume 16, Issue 2–3, pp 105–110 | Cite as

Protein synthesis in resting and stimulated human lymphocytes

  • Oscar Burrone
  • Israel D. Algranati
Article

Summary

The ribosomal profiles in lysates from resting and phytohemagglutinin stimulated human lymphocytes have been analyzed by sucrose gradient centrifugation. The percentage of polyribosomes increased during lymphocyte transformation reaching a maximal value of 60 to 70% of the total ribosomes after 72 hours of mitogen addition. This time period coincides with maximalin vivo protein synthesis. On the other hand, in nonstimulated lymphocytes, about 25% of the ribosomal particles appeared as aggregates, independently of the incubation period.

Experiments performed with homologous cell free systems containing ribosomes and supernatant fluids prepared from unstimulated or activated lymphocytes demonstrate that the mixtures containing both components from stimulated lymphocytes are several fold more active in polypeptide synthesis than the systems which contain ribosomal particles and cell sap from resting cells. Assays carried out with mixtures combining the components from both sources indicate that the increased activity depends on ribosomes as well as on the supernatant fractions.

Keywords

Sucrose Protein Synthesis Polypeptide Incubation Period Gradient Centrifugation 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Copper, H. L., 1973. In Effects of Drugs on the Cell Cycle (Zimmerman, A., Padilla, G. and Cameron, I., eds.), pp. 137–160, Academic Press, New York.Google Scholar
  2. 2.
    Kay, J. E., 1968. Eur. J. Biochem. 4, 225–232.Google Scholar
  3. 3.
    Kay, J. E., Ahern, T. and Atkins, M., 1971. Biochim. Biophys. Acta 247, 322–334.Google Scholar
  4. 4.
    Ahern, T. and Kay, J. E., 1973. Biochim. Biophys. Acta 331, 91–101.Google Scholar
  5. 5.
    Kay, J. E., Ahern, T., Lindsay, V. J. and Sampson, J., 1975. Biochim. Biophys. Acta 378, 241–250.Google Scholar
  6. 6.
    Ahern, T. and Kay, J. E., 1975. Exptl. Cell Res. 92, 513–515.Google Scholar
  7. 7.
    Ahern, T., Sampson, J. and Kay, J. E., 1974. Nature 248, 519–521.Google Scholar
  8. 8.
    Cooper, H. L., 1968. J. Biol. Chem. 243, 34–43.Google Scholar
  9. 9.
    Cooper, H. L., 1974. In Methods in Enzymology (Fleischer, S. and Packer, L., eds), Vol. 32B, pp. 633–636, Academic Press, New York.Google Scholar
  10. 10.
    Fridlender, B. R., Medrano, E. and Mordoh, J., 1974. Proc. Nat. Acad. Sci. U.S.A. 71, 1128–1132.Google Scholar

Copyright information

© Dr. W. Junk b.v. Publishers 1977

Authors and Affiliations

  • Oscar Burrone
    • 1
  • Israel D. Algranati
    • 1
  1. 1.Instituto de Investigaciones Bioquimicas “Fundación Campomar” and Facultad de Ciencias Exactas y NaturalesBuenos AiresArgentina

Personalised recommendations