Skip to main content

Purification of Human Erythrocyte Adenosine Deaminase

  • Chapter

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB))

Abstract

Adenosine deaminase (ADA) catalyzes the irreversible hydrolytic deamination of adenosine to produce inosine and ammonia (1). Extremely reduced or absent ADA activity in man is associated with one type of severe combined immunodeficiency (SCID) (2). Previous studies of normal ADA from a variety of species has provided evidence for substantial molecular heterogeneity. Multiple forms of ADA varying in molecular weight from 30,000 to 47,000 (designated small form) and 230,000 to 440,000 (designated large form) have been reported. (3–16).

This is a preview of subscription content, log in via an institution.

Buying options

Chapter
USD   29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD   39.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD   54.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Learn about institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Conway, E.J., and Cooke, R. (1939) Biochem. J. 331, 479–492.

    Google Scholar 

  2. Giblett, E.R., Anderson, J.E., Cohen, F., Pollara, B., and Meuwissen, H.J. (1972) Lancet 2, 1067–1069.

    Article  PubMed  CAS  Google Scholar 

  3. Ma, P.F., and Fisher, J.R. (1968) Comp. Biochem. Physiol. 27, 105–112.

    Article  PubMed  CAS  Google Scholar 

  4. Ma, P.F., and Fisher, J.R.(1968) Comp. Biochem. Physiol. 27, 687–694.

    Article  PubMed  CAS  Google Scholar 

  5. Ma, P.F., and Fisher, J.R.(1968) Biochem. Physiol. Acta 159, 153–159.

    CAS  Google Scholar 

  6. Murphy, P.M., Noonan, M., Collins, P., Tully, E., and Brady, T.G. (1969) Biochim. Biophys. Acta 171, 157–166.

    Article  PubMed  CAS  Google Scholar 

  7. Brady, T.G., and O’Connell, W. (1962) Biochim. Biophys. Acta 62216–229.

    Article  PubMed  CAS  Google Scholar 

  8. Pfrogner, N. (1967) Arch. Biochem. Biophys. 119, 141–146.

    Article  PubMed  CAS  Google Scholar 

  9. Cory, J.G., Weinbaum, G., and Suhadolnik, R.J. (1967) Arch. Biochem. Biophys. 118, 428–433.

    Article  PubMed  CAS  Google Scholar 

  10. Spencer, N., Hopkinson, D.A., and Harris, H. (1968) Ann. Hum. Genet. 32, 9–14.

    Article  Google Scholar 

  11. Ressler, N. (1969) Clin. Chim. Acta 24, 247–251.

    Article  PubMed  CAS  Google Scholar 

  12. Ma, P.F., and Fisher, J.R. (1969) Comp. Biochem. Physiol. 31, 771–781.

    Article  PubMed  CAS  Google Scholar 

  13. Akedo, H., Nishihara, H., Shinkai, K., and Komatsu, K., and Ishikawa, S. (1972) Biochim. Biophys. Acta 276, 257–271.

    Article  PubMed  CAS  Google Scholar 

  14. Osborne, W.R.A., and Spencer, N. (1973) Biochem. J. 133, 117–123.

    PubMed  CAS  Google Scholar 

  15. Van der Weyden, M.B., and Kelley, W.N. (1976) J. Biol. Chem., in press.

    Google Scholar 

  16. Piggott, C. O., and Brady, T.G. (1976) Biochim. Biophys. Acta 429, 600–607.

    Article  PubMed  CAS  Google Scholar 

  17. Van der Weyden, M.B., Buckley, R.H., and Kelley, W.N. (1974) Biochem Biophys. Res. Commun. 57, 590–595.

    Article  PubMed  CAS  Google Scholar 

  18. Hirschhorn, R., Beratis, N. and Rosen, R.S. (1975). Proc. Nat. Acad. Sci. USA. 73. 213–217.

    Article  Google Scholar 

  19. Chen, S., Scott, C.R. and Swedberg, K.R., (1975). Am. J. Hum. Genet. 27, 46–52.

    PubMed  CAS  Google Scholar 

  20. Rossi, C.A., Lucacchini, A., Montali, U., and Ronca, G. (1975) Int. J. Peptide Res. 7, 81–89.

    Article  CAS  Google Scholar 

  21. Daddona, P.E., and Kelley, W.N. (1976) J. Biol. Chem., in press.

    Google Scholar 

  22. Davis, B.J. (1964) Ann. N.Y. Acad. Sci. 121, 404–427.

    Article  PubMed  CAS  Google Scholar 

  23. Vesterberg, o., and Svensson, H. (1966) Acta Chem. Scand. 20. 820–834.

    Article  PubMed  CAS  Google Scholar 

  24. Cuatrecasas, P. (1970) J. Biol. Chem. 245, 3059–3065.

    PubMed  CAS  Google Scholar 

  25. Gilham, P.T., (1970) Methods Enzymol. 21, 191–197.

    Article  Google Scholar 

  26. Stevenson, K.J. and Landman, A. (1971) Can. J. Biochem. 49. 119–126.

    Article  PubMed  CAS  Google Scholar 

  27. Weber, K., and Osborn, M. (1969) J. Biol. Chem. 244, 4406–4412.

    PubMed  CAS  Google Scholar 

  28. Segrest, J.P. and Jackson, R.L. (1972) Methods Enzymol 28. 54–63.

    Article  Google Scholar 

  29. Ackers, G.K. (1967) J. Biol. Chem. 242, 3237–3238.

    CAS  Google Scholar 

  30. McCarty, K.S., Stafford, D., and Brown, O. (1968) Anal. Biochem. 24, 314–329.

    Article  PubMed  CAS  Google Scholar 

  31. Cohn, E.J. and Edsall, J.T. (1943) in “Proteins, Amino Acids, and Peptides”, pp. 370, Reinhold Publishing, New York.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1977 Plenum Press, New York

About this chapter

Cite this chapter

Daddona, P.E., Kelley, W.N. (1977). Purification of Human Erythrocyte Adenosine Deaminase. In: Müller, M.M., Kaiser, E., Seegmiller, J.E. (eds) Purine Metabolism in Man—II. Advances in Experimental Medicine and Biology. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-4223-6_28

Download citation

  • DOI: https://doi.org/10.1007/978-1-4613-4223-6_28

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-4225-0

  • Online ISBN: 978-1-4613-4223-6

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics