| Literature DB >> 21945700 |
Andriy E Zakalskiy1, Oksana M Zakalska1, Yuriy A Rzhepetskyy2, Natalia Potocka3, Oleh V Stasyk4, Daniel Horak5, Mykhailo V Gonchar6.
Abstract
Arginase (EC 3.5.3.1; L-arginine amidinohydrolase) is a key enzyme of the urea cycle that catalyses the conversion of arginine to ornithine and urea, which is the final cytosolic reaction of urea formation in the mammalian liver. The recombinant strain of the yeast Saccharomyces cerevisiae that is capable of overproducing arginase I (rhARG1) from human liver under the control of the efficient copper-inducible promoter CUP1, was constructed. The (His)(6)-tagged rhARG1 was purified in one step from the cell-free extract of the recombinant strain by metal-affinity chromatography with Ni-NTA agarose. The maximal specific activity of the 40-fold purified enzyme was 1600 μmol min(-1) mg(-1) protein. Copyright ÂEntities:
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Year: 2011 PMID： 21945700 DOI： 10.1016/j.pep.2011.09.001
Source DB: PubMed Journal: Protein Expr Purif ISSN： 1046-5928 Impact factor: 1.650