title: Purification and properties of rat small intestinal arginase.
abstract: 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...
mesh_terms: D000596:Amino Acids / Q000378:metabolism; D000818:Animals; D001119:Arginase / Q000302:isolation & purification / Q000378:metabolism; D004355:Drug Stability; D004492:Edetic Acid / Q000494:pharmacology; D006358:Hot Temperature; D007421:Intestine, Small / Q000201:enzymology*; D007668:Kidney / Q000201:enzymology; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D008297:Male; D008345:Manganese / Q000494:pharmacology; D008970:Molecular Weight; D051381:Rats; D014633:Valine / Q000494:pharmacology
chemical_list: D000596:Amino Acids; D008345:Manganese; D004492:Edetic Acid; D001119:Arginase; D014633:Valine