1991 年 55 巻 10 号 p. 2599-2605
An α-L-arabinosidase (α-L-arabinofuranoside arabinofuranohydrolase, EC 3.2.1.55) that can degrade both purified water soluble polysaccharide from soybean seeds and p-nitrophenyl-α-L-arabinofuranoside was purified 453-fold to near homogeneity from cotyledons of 4-day-old soybean seedlings.
The optimum pH and Km against p-nitrophenyl-α-L-arabinofuranoside of the purified enzyme were 4.8 and 0.53 mM, respectively. The enzyme was activated by Ca2+ and Zn2+ ions, but Cu2+, Hg2+, EDTA, and L-arabonic-γ-lactone inhibited the enzyme activity. The molecular weight of the enzyme subunit was estimated to be 87, 000 by SDS-PAGE.
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