Purification of arginase from Aspergillus nidulans.

A Dzikowska; J P Le Caer; P Jonczyk; P Wëgleński

doi:10.18388/abp.1994_4700

Purification of arginase from Aspergillus nidulans.

A Dzikowska Department of Genetics, Warsaw University, Poland.;
J P Le Caer
P Jonczyk
P Wëgleński

DOI: https://doi.org/10.18388/abp.1994_4700

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.

Published

1994-12-31

Issue

Vol. 41 No. 4 (1994)

Section

Articles

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