Advertisement

Enzyme-Loaded Erythrocytes

  • Garret Ihler
  • Robert Glew

Abstract

Erythrocytes, especially human erythrocytes, have been very extensively studied because of their medical interest and because they are conveniently obtained for biochemical and physiological studies. Mammalian erythrocytes lack nuclei which are pinched off from the cells when they pass through narrow orifices while escaping from the bone marrow. Once matured, they lack ribosomes and have lost the capability of protein synthesis. Because of their inability to renew themselves, the lifetime of normal human erythrocytes is restricted to about 120 days. Cell energy metabolism is restricted to glycolysis since the cells do not contain mitochondria. Their basic function is to serve as a container for hemoglobin. In this article we discuss a procedure for utilizing erythrocytes as containers for foreign proteins and enzymes as well as hemoglobin.

Keywords

Uric Acid Survival Characteristic Lysosomal Storage Disease Erythrocyte Ghost Hypotonic Medium 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Baker, R. F., 1967, Nature 215: 424–425.CrossRefGoogle Scholar
  2. Brady, R., Pentchev, P., Gal, A., Hibert, S., and Dekaban, A., 1974, New Engl. J. Med. 291: 989–993.CrossRefGoogle Scholar
  3. Chang, T. M. S., 1972, Artificial Cells, p. 52–66, Charles C. Thomas, Publisher, Springfield, Ill.Google Scholar
  4. Fiddler, M., Thorpe, S., Krivit, W., and Desnick, R., 1974, Enzyme therapy III, in vivo fate of erythrocyte entrapped ß-glucuronidase, in: Enzyme Therapy in Lysosomal Storage Disease (S. M. Tager, ed.), p. 182–185, North-Holland Publishing Co., Amsterdam.Google Scholar
  5. Hoffman, J. F., 1958, J. Gen. Physiol. 42: 9–28.CrossRefGoogle Scholar
  6. Ihler, G., Glow, R. and Ostling, F., 1973, Proc. Natl. Acad. Sci. V. S. 70: 1663–2666.Google Scholar
  7. Ihler, G., Lantzy, A., Purpura, J., and Glew, R., 1975, J. Clin. Invest. 56: 595–602.CrossRefGoogle Scholar
  8. Marsden, N. V. B., and Ostling, S. G., 1959, Nature 184: 723–724.CrossRefGoogle Scholar
  9. Pentchev, P., Brady, R., Hiffert, S., Gal, A., and Shapiro, D., 1973, J. Biol. Chem. 248: 5256–5261.Google Scholar
  10. Rifkind, R. A., 1966, Amer. J. Med. 41: 711–722.CrossRefGoogle Scholar
  11. Schrier, S. L., 1963, J. Clin. Invest. 42: 756–766.CrossRefGoogle Scholar
  12. Seeman, P., 1967, J. Cell. Biol. 32: 55–70.CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1977

Authors and Affiliations

  • Garret Ihler
    • 1
  • Robert Glew
    • 1
  1. 1.Department of BiochemistryUniversity of Pittsburgh School of MedicinePittsburghUSA

Personalised recommendations