Abstract
Arginase in yeast press juice was inactivated by dialysis at 0[degree] C, and could be reactivated by various metal ions. Liver arginase behaved like yeast arginase, but the dialysis at 0[degree] C. should be carried on for several wks. For reactivation, m/1000 solns. of Mn, Co, Ni, Cd and V were equally effective. Mn in m/300 000 soln. restored the original activity of the enzyme, while other ions were inactive at this conc. Arginase was considered to be an enzyme consisting of a protein carrier and Mn as activator or co-enzyme; it might function as a re-orienting-aminizing agent in protein synthesis.