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Human Adenosine Deaminase: Stoichiometry of the Large form Complex

  • Peter E. Daddona
  • William N. Kelley
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 122B)

Abstract

Adenosine deaminase (adenosine aminohydrolase, ADA, EC 3.5.4.4.) is widely distributed in human tissues. In some tissues ADA exists exclusively as the small molecular form (36,000–38,000) while in other tissues the large molecular form of the enzyme predominates (298,000).1 The small form of ADA has been purified to homogenity from human erythrocytes and was shown to be a single polypeptide of molecular weight 38,000.2,3 Physical and kinetic characteristics of small form ADA from various tissues appeared to be identical to the purified erythrocyte enzyme.1,2 The small form of the enzyme could be converted to the large form ADA by incubation with a specific ADA binding protein (BP) (also termed complexing protein or conversion factor).1,4,5 This purified binding protein from human kidney was shown to be a dimer of identical subunits with a native molecular weight of 190,000–200,000.4,5 The large form ADA produced in vitro was physically and kinetically indistinguishable from the native large form ADA from various tissues.1,4

Keywords

Adenosine Deaminase Large Form Small Form Radioactive Peak Native Molecular Weight 
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

  1. 1.
    M.B. Van der Weyden and W.N. Kelley, Human adenosine deaminase: distribution and properties. J. Biol. Chem. 251: 5448–5456 (1976).PubMedGoogle Scholar
  2. 2.
    P.E. Daddona and W.N. Kelley, Human adenosine deaminase: purification and subunit structure. J. Biol. Chem. 252: 110–115 (1977).PubMedGoogle Scholar
  3. 3.
    W.P. Schrader, A.R. Stacy and B. Pollara, Purification of human erythrocyte adenosine deaminase by affinity column chromatography. J. Biol. Chem. 251: 4026–4032 (1976).PubMedGoogle Scholar
  4. 4.
    P.E. Daddona and W.N. Kelley, Human adenosine deaminase binding protein: assay, purification and properties. J. Biol. Chem. 253: 4617–4623 (1978).PubMedGoogle Scholar
  5. 5.
    W.P. Schrader and A.R. Stacy, Purification and subunit structure of adenosine deaminase from human kidney. J. Biol. Chem. 252: 6409–6415 (1977).PubMedGoogle Scholar

Copyright information

© Plenum Press, New York 1980

Authors and Affiliations

  • Peter E. Daddona
    • 1
  • William N. Kelley
    • 1
  1. 1.Department of Internal Medicine and Biological Chemistry, Human Purine Research CenterUniversity of Michigan Medical SchoolAnn ArborUSA

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