Purification of arginase from Aspergillus nidulans
Dzikowska, A.; Le Caer, J.P.; Jonczyk, P.; Wëgleński, P.
Acta Biochimica Polonica 41(4): 467-471
1994
ISSN/ISBN: 0001-527X PMID: 7732765 Document Number: 434013
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.