Advertisement

Properties of a Novel PEG Derivative of Calf Adenosine Deaminase

  • Charles Beauchamp
  • Peter E. Daddona
  • David P. Menapace
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 165)

Abstract

Human adenosine deaminase (ADA) deficiency has been causally associated with severe combined immunodeficiency diseasel. Some success has been achieved in restoring immune function in these patients by administering the enzyme via red blood cell transfusions2. A derivative of ADA which retains enzymatic activity and which has a long circulation time and minimal immunogenicity when injected intravenously could be useful as an alternate means of enzyme replacement therapy.

Keywords

Enzyme Replacement Therapy Adenosine Deaminase Blood Clearance Severe Combine Immunodeficiency Severe Combine Immunodeficiency Disease 
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.
    B.S. Mitchell and W.N. Kelley, Purinogenic immunodeficiency diseases: Clinical features and molecular mechanisms, Ann. Int. Med., 92: 826 (1980).PubMedGoogle Scholar
  2. 2.
    S.H. Polmar, Enzyme replacement and other biochemical approaches to the therapy of adenosine deaminase deficiency, Ciba Foundation Symposium 68: 213 (1978).PubMedGoogle Scholar
  3. 3.
    A. Abuchowski, J.R. McCoy, N.C. Palczuk, T. van Es and F.F. Davis, Effect of coualent attachement of polyethylene glycol on immunogenicity and circulating life of bovine liver catalase, J. Biol. Chem., 252: 3582 (1977).PubMedGoogle Scholar
  4. 4.
    S. Davis, Y.K. Park, A. Abuchowski, and F.F. Davis, Hypouricemic effect of polyethylene glycol modified urate oxidase, Lancet 2: 281 (1981).Google Scholar
  5. 5.
    G.S. Bethell, J.S. Ayers, W.S. Hancock, and M.T.W. Hearn, A novel method of activation of cross-linked agaroses with 1,1’-carbonyldiimidazole which gives a matrix for affinity chromatography devoid of additional charged groups, J. Biol. Chem. 254: 2572 (1979).Google Scholar
  6. 6.
    C. Beauchamp, D. Menapace, S. Gonias and S. Pizzo, Manuscript in preparation (1982).Google Scholar
  7. 7.
    A.N. Glazer, R.J. Delange and D.S. Sigman, Chemical Modification of Proteins American Elsevier Publishing Co., New York (1975).Google Scholar
  8. 8.
    M.B. van der Weyden, R.H. Buckley and W.N. Kelley, Molecular forms of adenosine deaminase in severe combined immunodeficiency, Biochem. Biophys. Res. Comm., 57: 590 (1974).Google Scholar
  9. 9.
    B.E. Chechik, W.P. Schrader and P.E. Daddona, Identification of human thymus-leukemia-associated antigen as a low-molecular-weight form of adenosine deaminase, J. Natl. Cancer Inst. 64: 1077 (1980).PubMedGoogle Scholar
  10. 10.
    K.J. Wider, N.C. Palczuk, T. van Es and F.F. Davis, Some properties of polyethylene glycol: phenylalanine ammonia-lyase adducts, J. Biol. Chem., 254: 12579 (1979).Google Scholar
  11. 11.
    G.O. Till, C. Beauchamp, W. Tourtellotte Jr., D. Menapace, R. Kunkel, K.J. Johnson and P.A. Ward, Oxygen radical dependent lung damage following thermal injury of rat skin, J. Clin. Invest. manuscript submitted (1982).Google Scholar

Copyright information

© Plenum Press, New York 1984

Authors and Affiliations

  • Charles Beauchamp
    • 1
  • Peter E. Daddona
    • 1
  • David P. Menapace
    • 1
  1. 1.Department of Internal MedicineUniversity of Michigan Medical School and Ann Arbor Veterans Administration Medical CenterAnn ArborUSA

Personalised recommendations