Adenosine aminohydrolase activity in the regenerating rat liver.
The specific activity of adenosine aminohydrolase in the regenerating rat liver is significantly increased 12 h after partial hepatectomy. There is a twofold increase in enzyme activity at 48 h, after which the activity begins to decline. However, increased values still persist 7 days postsurgery. The enzyme is located mainly in the soluble supernatant (90-95%) of the cell. The purified enzyme from 48-h regenerating liver and control liver has similar kinetic properties (Km 54-58 microM for adenosine), similar molecular weights (30,000-35,000), and are equally inhibited by an irreversible transition-state analog and a reversible competitive inhibitor. It is concluded that adenosine aminohydrolase in regenerating liver is an integral component of a salvage pathway designed for the reutilization of nucleotides, and thus helps maintain a "growth state" for the regenerating liver.
D000243:Adenosine Deaminase / Q000378:metabolism*; D000818:Animals; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008115:Liver Regeneration; D008297:Male; D009700:Nucleoside Deaminases / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D013379:Substrate Specificity
D009700:Nucleoside Deaminases; D000243:Adenosine Deaminase