Substrate Specificity of α-Glucuronidase Isolated from Snail Acetone Powder
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概要
- 論文の詳細を見る
The substrate speciticity of a p-nitrophenyl α-D-glucopyranosyl-uronic acid-hydrolyzinig enzyme (PNP-GAase) isolated from snail acetone powder has been investigated with various substrates, such as P-nitrophenyl α-D-glucopyranosyluronic acid (PNP-GA), 2-O-α-D-glucopyraniosyluronic acid-D-xylose (GA-2X), 2-O-(4-O-methyl-α-D-glucopyranosyluronic acid)-D-xylose (MeGA-2X), and O-α-D-glucopyranosyluronic acid-α-D-glucopyranosiduronic acid (GA-GA). The K_m (mM) and V_<max> (μmol of glucuronic acid formed/mg of en-zyme protein/min) toward these substrates were as follows; 0.13 and 3.21 for PNP-GA, 0.33 and 0.089 for GA-2X, 17.6 and 0.094 for MeGA-2X, and 0.36 and 0.015 for GA-GA, respectively. The results indicate that the PNP-GAase specifically hydrolyzed PNP-GA, however, the enzyme had broad substrate specificity.
- 社団法人日本農芸化学会の論文
- 1996-03-23
著者
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Kusakabe Isao
Institute of Applied Biochemistry, University of Tsukuba
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Kawabata Yasuyuki
Institute of Applied Biochemistry, University of Tsukuba
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Kuno Atsushi
Research Center For Medical Glycoscience National Institute Of Advanced Industrial Science And Techn
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KUNO Atsushi
Institute of Applied Biochemistry, University of Tsukuba
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Kuno A
Yamagata Univ. Yamagata Jpn
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GAMA Yasuo
National Institute of Materials and Chemical Research
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Gama Y
National Inst. Advanced Industrial Sci. And Technol. (aist) Ibaraki Jpn
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Gama Yasuo
National Chemical Laboratory For Industry
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Kusakabe I
Univ. Tsukuba Tsukuba Jpn
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Koyama Y
National Inst. Biosci. & Human Technol. Tsukuba Science City Jpn
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Kusakabe Isao
Institute Of Applied Biochemistry University Of Tsukuba
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Kawabata Y
Univ. Tsukuba Ibaraki Jpn
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Kawabata Yasuyuki
Institute Of Applied Biochemistry University Of Tsukuba
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