Adenylate deaminase from rat muscle. Regulation by purine nucleotides and orthophosphate in the presence of 150 mM KCl.

摘要: Adenylate deaminase from rat skeletal muscle has been studied with the objective of understanding how activity enzyme is regulated in vivo. ATP and GTP inhibit at low concentrations presence 150 mM KCl. The inhibition reversed as concentration raised to physiological levels. unphysiologically high In ATP, also greatly diminished, but by orthophosphate remains strong. apparent affinities for GTP, are reduced pH decreased 7.0 6.2. ADP reduces inhibitors. regulatory effects produced primarily their unchelated forms. Comparison kinetic behavior vitro metabolite vivo indicates that major variables regulate adenylate AMP, ADP, orthophosphate, H+.