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Adenosine Deaminase: Characterization of the Molecular Heterogeneity of the Enzyme in Human Tissue

  • M. B. Van der Weyden
  • W. N. Kelley
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. In human tissue this activity exhibits considerable molecular heterogeneity in that “tissue specific isoenzymes” have been demonstrated with either starch gel electrophoresis (1–3) or gel filtration (3,4,7). The molecular weights of the multiple forms apparent have varied from 30,000 to 47,000 (3–7) and 230,000 to 440,000 (3,4,7). Although the basis for this heterogeneity has been obscure, with definition of the characteristics of residual ADA activity in tissues of patients with severe combined immunodeficiency and ADA deficiency (8,9), it has been proposed that the molecular heterogeneity of ADA in human tissue is the result of post-translational modification of a single locus product (9). For this hypothesis to be valid, interconvertibility between the molecular forms of ADA should be demonstrated. In this study we have examined the nature of the molecular heterogeneity of ADA in human tissue and demonstrate that the forms evident are interconvertible.

Keywords

Tissue Extract Adenosine Deaminase Large Form Severe Combine Immunodeficiency Small Form 
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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Copyright information

© Plenum Press, New York 1977

Authors and Affiliations

  • M. B. Van der Weyden
    • 1
    • 2
  • W. N. Kelley
    • 1
    • 2
  1. 1.Department of MedicineMonash UniversityAustralia
  2. 2.Department of MedicineUniversity of MichiganAnn ArborUSA

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