Purification and properties of rat small intestinal arginase

Arginase [L-arginine amidinhydrolase EC 3.5.3.1] from rat small intestine was purified about 2,200-fold and its properties were compared with those of the rat liver and kidney enzymes. Intestinal arginase was extremely labile on storage either at -10 degrees or 4 degrees and lost activity during purification unless 25 mM L-valine was present. The purified enzyme appeared to be homogeneous by disc electrophoresis and its molecular weight was estimated to be 120,000 by Sephadex G-100 filtration...