Purification and Properties of an alpha-L-Arabinofuranosidase from Cotyledons of Soybean Seedlings(Biological Chemistry)
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概要
- 論文の詳細を見る
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 K_m against p-nitrophenyl-α-L-arabinofuranoside of the purified enzyme were 4.8 and 0.53 mM, respectively. The enzyme was activated by Ca^<2+> and Zn^<2+> ions, but Cu^<2+>, Hg^<2+>, 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.
- 社団法人日本農芸化学会の論文
- 1991-10-23
著者
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Tajima Shigeyuki
Department of Bioresource Science, Faculty of Agriculture, Kagawa University
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Tajima Shigeyuki
Department Of Agricultural Chemistry Faculty Of Agriculture Nagoya University
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HATANAKA Hakuei
Research Institute of Agricultural Resources, Ishikawa Agricultural College
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IMAOKA Hideyuki
Environment Department, Takamatsu City Office
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KASAI Tadasi
Department of Bioresource Science, Faculty of Agriculture, Kagawa University
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Kasai Tadasi
Department Of Bioresource Science Faculty Of Agriculture Kagawa University
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Imaoka Hideyuki
Environment Department Takamatsu City Office
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Hatanaka Hakuei
Research Institute Of Agricultural Resources Ishikawa Agricultural College
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