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Characterization of Adenosine Deaminating Activity in Normal and Adenosine Deaminase Deficient Human Tissue

  • Martin B. Van Der Weyden
  • Ian Jack
  • John B. Ziegler
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 165)

Abstract

The differing properties of residual enzyme activity converting adenosine to inosine in tissue of individuals with adenosine deaminase deficiency and severe combined immunodeficiency (1–5) reflect in part the limited amount of enzyme activity in these tissues and the molecular heterogeneity of adenosine deaminase in normal tissue. Human adenosine deaminase exists either as a particulate species or as one of two soluble interconvertible molecular forms designated the small and large forms (6). The large form of adenosine deaminase (Mr 280,000) is composed of two molecules of the small form (Mr 38,000) and one molecule of complexing protein (Mr 200,000) (6,7). In addition to these forms, analysis of normal tissue has revealed a low level of intermediate (Mr 110,000) activity (6) which in splenic tissue of an individual with adenosine deaminase deficiency and severe combined immunodeficiency was the exclusive form of adenosine deaminating activity (1). Subsequently Schrader et al (4) and Daddona and Kelley (5) have demonstrated with either splenic tissue or B lymphoblast derived from adenosine deaminase normal or deficient individuals, the presence of an aminohydrolase which differs from normal adenosine deaminase in its Km for adenosine, pH optimum, insensitivity to the potent adenosine deaminase inhibitor erythro-9-(2 hydroxy-3-nonyl)-adenine (EHNA) and its immunoreactivity with antibody to human adenosine deaminase. In this communication we report our findings on this distinct aminohydrolase in normal and adenosine deaminase deficient tissue.

Keywords

Enzyme Replacement Therapy Adenosine Deaminase Residual Enzyme Activity Severe Combine Immunodeficiency Splenic Tissue 
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.

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References

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Copyright information

© Springer Science+Business Media New York 1984

Authors and Affiliations

  • Martin B. Van Der Weyden
    • 1
    • 2
    • 3
  • Ian Jack
    • 1
    • 2
    • 3
  • John B. Ziegler
    • 1
    • 2
    • 3
  1. 1.Department of MedicineMonash University, Alfred HospitalPrahranAustralia
  2. 2.Department of VirologyRoyal Children’s HospitalParkvilleAustralia
  3. 3.Department of Pediatric ImmunologyPrince of Wales Hospital RandwickNew South WalesAustralia

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