Kinds of Glycosidase and Properties of β-N-Acetylglucosaminidase Bound to Mycelia of Streptomyces sp.
スポンサーリンク
概要
- 論文の詳細を見る
An extract liberated from mycelia of the L-13 strain of Streptomyces by 0.2 M phosphate buffer, pH 6.5,contained β-N-acetylglucosaminidase, β-N-acetylgalactosaminidase and a little α-glucosidase. On chromatofocusing, the isoelectric point of β-N-acetylglucosaminidase was around pH 8.1. The enzyme prepared thus was homogeneous, and had both β-N-acetylglucosaminidase and β-N-acetylgalactosaminidase activities. The β-N-acetylglucosaminidase was most active at pH 6.0 and stable between pH 4 to 8. The K_m value for p-nitorphenyl β-N-acetylglucosaminide was 0.25 mM N-Acetylglucosaminolactone was the most potent inhibitor tested.
- 社団法人日本生物工学会の論文
- 1987-10-25
著者
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Sasaki Takeshi
Department of Rheumatology, Tohoku University school of Medicine
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Okiura Tatsuyuki
Department Of Agricultural Chemistry Faculty Of Agriculture Ehime University
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IWAMOTO TOORU
Department of Agricultural Chemistry, Faculty of Agriculture, Ehime University,
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INAOKA MEGUMU
Department of Agricultural Chemistry, Faculty of Agriculture, Ehime University,
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Sasaki Takeshi
Department Of Biotechnology College Of Agriculture Ehime University
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Iwamoto Tooru
Department Of Agricultural Chemistry Faculty Of Agriculture Ehime University
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Inaoka M
Department Of Agricultural Chemistry Faculty Of Agriculture Ehime University
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Inaoka Megumu
Department Of Agricultural Chemistry Faculty Of Agriculture Ehime University
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Sasaki Takeshi
Department Of Agricultural Chemistry Faculty Of Agriculture Ehime University
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