Characterization and purification of adenosine deaminase 1 from human and chicken liver

Comp Biochem Physiol B Biochem Mol Biol. 2002 Oct;133(2):173-82. doi: 10.1016/s1096-4959(02)00122-7.

Abstract

Adenosine deaminase 1 (ADA1) was purified from human and chicken liver. The purified enzyme had a molecular weight of approximately 42,000 Da on SDS-PAGE. In humans, ADA1 was mainly purified concomitant with ADA-binding protein, dipeptidyl peptidase IV (DPP IV)/CD26; however, in chickens, only ADA1 without DPP IV was purified. Both human and chicken ADA1s showed similar properties on substrate specificities, sensitivities on inhibitors, and pH profile. However, they had different affinities with adenosine-Sepharose and IgG anti-ADA1-Sepharose. Human ADA1 was not adsorbed in adenosine-Sepharose column, but chicken ADA1 was adsorbed. As for IgG anti-ADA1-Sepharose column, the results were converse. Furthermore, human ADA1 could bind to DPP IV whereas chicken ADA1 could not.

Publication types

  • Comparative Study

MeSH terms

  • Adenosine / metabolism
  • Adenosine Deaminase / chemistry*
  • Adenosine Deaminase / isolation & purification*
  • Adenosine Deaminase / metabolism
  • Animals
  • Antibodies / metabolism
  • Blotting, Western
  • Chickens
  • Dipeptidyl Peptidase 4 / metabolism
  • Enzyme Inhibitors / pharmacology
  • Humans
  • Hydrogen-Ion Concentration
  • Liver / enzymology*
  • Protein Binding
  • Substrate Specificity

Substances

  • Antibodies
  • Enzyme Inhibitors
  • Dipeptidyl Peptidase 4
  • Adenosine Deaminase
  • Adenosine