Advertisement

Purification of Human Erythrocyte Adenosine Deaminase

  • P. E. Daddona
  • W. N. Kelley
Chapter
Part of the Advances in Experimental Medicine and Biology book series

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).

Keywords

Human Erythrocyte Adenosine Deaminase Severe Combine Immunodeficiency Sedimentation Coefficient Partial Specific Volume 
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. 1.
    Conway, E.J., and Cooke, R. (1939) Biochem. J. 331, 479–492.Google Scholar
  2. 2.
    Giblett, E.R., Anderson, J.E., Cohen, F., Pollara, B., and Meuwissen, H.J. (1972) Lancet 2, 1067–1069.PubMedCrossRefGoogle Scholar
  3. 3.
    Ma, P.F., and Fisher, J.R. (1968) Comp. Biochem. Physiol. 27, 105–112.PubMedCrossRefGoogle Scholar
  4. 4.
    Ma, P.F., and Fisher, J.R.(1968) Comp. Biochem. Physiol. 27, 687–694.PubMedCrossRefGoogle Scholar
  5. 5.
    Ma, P.F., and Fisher, J.R.(1968) Biochem. Physiol. Acta 159, 153–159.Google Scholar
  6. 6.
    Murphy, P.M., Noonan, M., Collins, P., Tully, E., and Brady, T.G. (1969) Biochim. Biophys. Acta 171, 157–166.PubMedCrossRefGoogle Scholar
  7. 7.
    Brady, T.G., and O’Connell, W. (1962) Biochim. Biophys. Acta 62216–229.PubMedCrossRefGoogle Scholar
  8. 8.
    Pfrogner, N. (1967) Arch. Biochem. Biophys. 119, 141–146.PubMedCrossRefGoogle Scholar
  9. 9.
    Cory, J.G., Weinbaum, G., and Suhadolnik, R.J. (1967) Arch. Biochem. Biophys. 118, 428–433.PubMedCrossRefGoogle Scholar
  10. 10.
    Spencer, N., Hopkinson, D.A., and Harris, H. (1968) Ann. Hum. Genet. 32, 9–14.CrossRefGoogle Scholar
  11. 11.
    Ressler, N. (1969) Clin. Chim. Acta 24, 247–251.PubMedCrossRefGoogle Scholar
  12. 12.
    Ma, P.F., and Fisher, J.R. (1969) Comp. Biochem. Physiol. 31, 771–781.PubMedCrossRefGoogle Scholar
  13. 13.
    Akedo, H., Nishihara, H., Shinkai, K., and Komatsu, K., and Ishikawa, S. (1972) Biochim. Biophys. Acta 276, 257–271.PubMedCrossRefGoogle Scholar
  14. 14.
    Osborne, W.R.A., and Spencer, N. (1973) Biochem. J. 133, 117–123.PubMedGoogle Scholar
  15. 15.
    Van der Weyden, M.B., and Kelley, W.N. (1976) J. Biol. Chem., in press.Google Scholar
  16. 16.
    Piggott, C. O., and Brady, T.G. (1976) Biochim. Biophys. Acta 429, 600–607.PubMedCrossRefGoogle Scholar
  17. 17.
    Van der Weyden, M.B., Buckley, R.H., and Kelley, W.N. (1974) Biochem Biophys. Res. Commun. 57, 590–595.PubMedCrossRefGoogle Scholar
  18. 18.
    Hirschhorn, R., Beratis, N. and Rosen, R.S. (1975). Proc. Nat. Acad. Sci. USA. 73. 213–217.CrossRefGoogle Scholar
  19. 19.
    Chen, S., Scott, C.R. and Swedberg, K.R., (1975). Am. J. Hum. Genet. 27, 46–52.PubMedGoogle Scholar
  20. 20.
    Rossi, C.A., Lucacchini, A., Montali, U., and Ronca, G. (1975) Int. J. Peptide Res. 7, 81–89.CrossRefGoogle Scholar
  21. 21.
    Daddona, P.E., and Kelley, W.N. (1976) J. Biol. Chem., in press.Google Scholar
  22. 22.
    Davis, B.J. (1964) Ann. N.Y. Acad. Sci. 121, 404–427.PubMedCrossRefGoogle Scholar
  23. 23.
    Vesterberg, o., and Svensson, H. (1966) Acta Chem. Scand. 20. 820–834.PubMedCrossRefGoogle Scholar
  24. 24.
    Cuatrecasas, P. (1970) J. Biol. Chem. 245, 3059–3065.PubMedGoogle Scholar
  25. 25.
    Gilham, P.T., (1970) Methods Enzymol. 21, 191–197.CrossRefGoogle Scholar
  26. 26.
    Stevenson, K.J. and Landman, A. (1971) Can. J. Biochem. 49. 119–126.PubMedCrossRefGoogle Scholar
  27. 27.
    Weber, K., and Osborn, M. (1969) J. Biol. Chem. 244, 4406–4412.PubMedGoogle Scholar
  28. 28.
    Segrest, J.P. and Jackson, R.L. (1972) Methods Enzymol 28. 54–63.CrossRefGoogle Scholar
  29. 29.
    Ackers, G.K. (1967) J. Biol. Chem. 242, 3237–3238.Google Scholar
  30. 30.
    McCarty, K.S., Stafford, D., and Brown, O. (1968) Anal. Biochem. 24, 314–329.PubMedCrossRefGoogle Scholar
  31. 31.
    Cohn, E.J. and Edsall, J.T. (1943) in “Proteins, Amino Acids, and Peptides”, pp. 370, Reinhold Publishing, New York.Google Scholar

Copyright information

© Plenum Press, New York 1977

Authors and Affiliations

  • P. E. Daddona
    • 1
  • W. N. Kelley
    • 1
  1. 1.Department of Internal Medicine and Biological ChemistryUniversity of Michigan Medical SchoolAnn ArborUSA

Personalised recommendations