Purification and Characterization of Dioscin-α-L-rhamnosidase from Pig Liver

概要

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Dioscin-α-L-rhamnosidase was isolated, purified and partially characterized from pig liver. The maximum activity was reached at pH 7, 42℃, 24h, and 2% of substrate concentration. Fe^<3+> and Cu^<2+> inhibited the enzyme; the ion Ca^<2+> activated it. Mg^<2+> was an inhibitor at 100mM, but it was an activator at 200mM. Zn^<2+> could be a weak activator of the enzyme. The molecular weight of dioscin-α-L-rhamnosidase was about 47kDa as determined by the method of SDS-polyacrylamide gel electrophoresis.
公益社団法人日本薬学会の論文
2005-08-01