Properties of α-Mannosidase Partially Purified from the Apple Snail, Pomacea canaliculata
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概要
- 論文の詳細を見る
Pomacea canaliculata α-mannosidase (260 kDa), composed of at least two isoforms with different pI, was partially purified. The activity was maximum at pH 4 and unaltered after incubation at 60℃ for 60 min. ZnCl_2,CaCl_2 and EDTA inhibited it . The enzyme catalyzed the hydrolysis of α1-2,α1-3,and α1-6 mannosidic linkages.
- 社団法人日本農芸化学会の論文
- 1998-11-23
著者
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ASO yoichi
Laboratory of Protein Chemistry & Engineering, Kyushu University
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ISHIGURO Masatsune
Laboratory of Protein Chemistry and Engineering, Kyushu University Graduate School of Bioresource an
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Hirata K
Laboratory Of Protein Chemistry And Engineering Graduate School Of Genetic Resources Technology Kyus
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Aso Y
Institute Of Genetic Resources Graduate School Of Bioresources And Bioenvironmental Science Kyushu U
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HIRATA Koji
Laboratory of Protein Chemistry and Engineering, Graduate School of Genetic Resources Technology, Ky
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Ishiguro M
Laboratory Of Insect Genetic Resources Faculty Of Agriculture Kyushu University
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Ishiguro Masatsune
Laboratory Of Protein Chemistry & Engineering Department Of Genetic Resources Technology Facultr
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Ishiguro M
Suntory Institute For Bioorganic Research
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Ishiguro Masatsune
Laboratory of Insect Genetic Resources, Faculty of Agriculture, Kyushu University
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ASO Yoichi
Laboratory of Genetic and Protein Engineering, Faculty of Agriculture, Kyushu University
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