Purification of arginase from Aspergillus nidulans

• Autorzy: Dzikowska A. , Le Caer J.P. , Jonczyk P. , Weglenski P.
• Języki publikacji: EN

Abstrakty

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 crussa (38.3 kDa) and Saccharomyces cerevisiae (39 kDa) enzymes. The native molecular mass of arginase is 125 kDa. The subunit/nati ve 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.

Słowa kluczowe

EN

Aspergillus nidulans; purification; arginase

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 1994
• Tom: 41
• Numer: 4
• Opis fizyczny: p.467-471,fig.

Twórcy

autor

Dzikowska A.

• Warsaw University, A.Pawinskiego 5a, 02-106 Warsaw, Poland

autor

Le Caer J.P.

autor

Jonczyk P.

autor

Weglenski P.

Bibliografia

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