Purification of arginase from Aspergillus nidulans. | Zendy

Agnieszka Dzikowska | Zendy; Jean Pierre Le Caer | Zendy; Piotr Jonczyk | Zendy; Piotr Węgleński | Zendy

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Purification of arginase from Aspergillus nidulans.

Author(s) -

Agnieszka Dzikowska,

Jean Pierre Le Caer,

Piotr Jonczyk,

Piotr Węgleński

Publication year - 1994

Publication title -

acta biochimica polonica

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.452

H-Index - 78

eISSN - 1734-154X

pISSN - 0001-527X

DOI - 10.18388/abp.1994_4700

Subject(s) - arginase , aspergillus nidulans , neurospora crassa , molecular mass , protein subunit , biochemistry , enzyme , biology , homology (biology) , arginine , aspergillus fumigatus , chemistry , amino acid , gene , microbiology and biotechnology , mutant

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.

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