Adenosine deaminase 2 from chicken liver: purification, characterization, and N-terminal amino acid sequence

Comp Biochem Physiol B Biochem Mol Biol. 2004 Feb;137(2):247-54. doi: 10.1016/j.cbpc.2003.11.010.


Adenosine deaminase (ADA) is involved in purine metabolism and plays an important role in the mechanism of the immune system. ADA activity is composed of two kinetically distinct isozymes, which are referred to as ADA1 and ADA2. ADA1 is widely distributed in many animals and well characterized. On the contrary, relatively little is known about ADA2. In this study, we first purified ADA2 to homogeneity from chicken liver. The purified enzyme had a molecular mass of approximately 110 kDa on gel filtration. Also, the enzyme was shown to be a homodimer with an estimated molecular mass of 61 kDa on SDS-PAGE. Following treatment with N-glycosidase, the molecular mass of ADA2 changed to 55 kDa. Several properties of the highly purified ADA2 were also investigated in this study. Furthermore, the N-terminal amino acid sequence of ADA2 was determined.

MeSH terms

  • Adenine / analogs & derivatives*
  • Adenine / pharmacology
  • Adenosine Deaminase / chemistry*
  • Adenosine Deaminase / isolation & purification*
  • Adenosine Deaminase Inhibitors
  • Amino Acid Sequence
  • Animals
  • Chickens
  • Enzyme Inhibitors / pharmacology
  • Enzyme Stability
  • Isoenzymes
  • Liver / enzymology*
  • Molecular Sequence Data
  • Pentostatin / pharmacology
  • Protein Structure, Quaternary
  • RNA-Binding Proteins
  • Sequence Analysis, Protein
  • Substrate Specificity


  • Adenosine Deaminase Inhibitors
  • Enzyme Inhibitors
  • Isoenzymes
  • RNA-Binding Proteins
  • Pentostatin
  • 9-(2-hydroxy-3-nonyl)adenine
  • ADARB1 protein, human
  • Adenosine Deaminase
  • Adenine