Purification and properties of human liver pyruvate carboxylase

MC Scrutton, MD White - Biochemical medicine, 1974 - Elsevier
Pyruvate carboxylase has been purified from human liver to a specific activity of 10.5
units/mg and a purity of approximately 30% as judged by polyacrylamide-gel
electrophoresis. The human liver enzyme has been shown to exhibit significant catalytic
activity in the absence of the positive effector acetyl-CoA; and the catalytic properties of the
acetyl-CoA-dependent and acetyl-CoA-independent activities have been defined. Human
liver pyruvate carboxylase is activated by monovalent cations with K+, NH 4+, and Rb+ as …