title: Purification of arginase from Aspergillus nidulans.
abstract: Arginase (EC 3.5.3.1) of Aspergillus nidulans, the enzyme which enables the fungus to use arginine as the sole nitrogen source was purified to homogeneity. Molecular mass of the purified arginase subunit is 40 kDa and is similar to that reported for the Neurospora crassa (38.3 kDa) and Saccharomyces cerevisiae (39 kDa) enzymes. The native molecular mass of arginase is 125 kDa. The subunit/native molecular mass ratio suggests a trimeric form of the protein. The arginase protein was cleaved and partially sequenced. Two out of the six polypeptides sequenced show a high degree of homology to conserved domains in arginases from other species.
authors.affiliation: Department of Genetics, Warsaw University, Poland.
authors.forename: A
authors.initials: A
authors.lastname: Dzikowska
authors.forename: J P
authors.initials: JP
authors.lastname: Le Caer
authors.forename: P
authors.initials: P
authors.lastname: Jonczyk
authors.forename: P
authors.initials: P
authors.lastname: Wëgleński
mesh_terms: D000595:Amino Acid Sequence; D001119:Arginase / Q000302:isolation & purification*; D001233:Aspergillus nidulans / Q000201:enzymology*; D017124:Conserved Sequence; D008969:Molecular Sequence Data; D008970:Molecular Weight; D016415:Sequence Alignment
chemical_list: D001119:Arginase