Journal archive > 2010 > N 6 November-December

???HUMAN ARGINASE I FROM THE RECOMBINANT YEAST Hansenula polymorpha:
ISOLATION AND?CHARACTERIZATION OF?THE?ENZYME

N. Ye. Stasyuk1,2, G. Z. Gayda1, Y.? P.? Koval’chuk2, O. V. Stasyk1, M.? V.? Gonchar1

1Institute of Cell Biology, National Academy of Sciences of Ukraine, Lviv;
2Ivan Franko L’viv National University, Ukraine;
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Purified human arginase I preparations homogeneous in SDS-PAAG test were obtained by the affinity chromatography on the synthesized sorbent L-arginine-macroporous glass.
Some physico-chemical characteristics of the isolated arginase preparation have been estimated: thermo- and pH-stability, temperature- and pH-optima of the enzymе. The influence of some bivalent metal ions and other additives on enzymatic activity for stabilization of the enzyme and optimization of its storage conditions was studied.

Key words: recombinant yeast Hansenula polymorpha, human arginase I, L-arginine, affinity sorbent.

The original article in Ukrainian is available for download in PDF format.