Function of MannanChains of Yeast Repressible Acid Phosphatase on Its Enzymatic Properties
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概要
- 論文の詳細を見る
To find the function of the mannanchains covalently attached to yeast repressible acid phosphatase, the N-glycosidic carbohydrate chains were removed by endo-β-N-acetylglucosaminidase H under native conditions. Almost all of the N-glycosidic mannan chains were cleaved off by the glycosidase. The deglycosylated enzyme was shown to be a dimer structure as is the native enzyme. The deglycosylated enzyme retained enzyme activity, the same Km, and the same circular dichroism spectra as the native enzyme. These results indicate that the carbohydrate chains are not essential for maintaining the active enzyme structure, but the deglycosylated enzyme was shown to be more sensitive to acidic pHand high temperature.
- 社団法人 日本農芸化学会の論文
著者
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MIZUNAGA Takemitsu
Department of Agricultural Chemistry, Faculty of Agriculture, The University of Tokyo
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Maruyama Yoshiharu
Department Of Agricultural Chemistry Faculty Of Agriculture The University Of Tokyo
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OSHIDA Tadahiro
Department of Agricultural Chemistry, Faculty of Agriculture, The University of Tokyo
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TAKASAKI Akiko
Department of Agricultural Chemistry, Faculty of Agriculture, The University of Tokyo
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