Purification and Some Properties of a β-Xylosidase and an α-Fucosidase from Apple Snails (Pomacea canaliculata)

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概要

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• β-Xylosidase andα-fucosidase were purified from the viscera of apple snails (Pomacea canaliculata)using ammonium sulfate precipitation, hydrophobic chromatography on Butyl-Toyopearl, gel filtration on Sephacryl S-300, and Q-Sepharose column chromatography. β-Xylosidase andα-fucosidase are glycoproteins and their molecular masses were estimated to be approximately 85 kDa and 54 kDa by SDS-polyacrylamide gel electrophoresis, and assumed to be about 96 kDa and 230 kDa from their sedimentation coefficients, respectively, indicating that the former is a monomer and the latter has a tetrameric structure. β-Xylosidase is stable at pH 4-10 and its optimum pH toward pNP-β-D-xyloside is around 3:6, whileα-fucosidase is fairly stable at 65℃ and pH 4-10, and its optimum pHs toward pNP-α-L-fucoside are around 3.2 and 5.2.β-Xylosidase released a xylose residue from Xylβ1→2Manβ1→4GlcNAcβ1→4(Fucα1→3)GlcNAc-PA and Manα1→6(Manα1→3)(Xylβ1→2)Manβ1→4GlcNAcβ1→4(Fucα1→3)GlCNAc-PA, but not from GlcNAcβ1→ 2Manα1→6(GlcNAcβ1→2Manα1→3)(Xylβ1→2)Manβ1→4GlcNAcβ1→4(Fucα1→3)GlcNAc-PA, whileα-fucosidase released a fucose residue from these three PA-oligosaccharides.

• 社団法人日本農芸化学会の論文
• 1996-02-23

著者

• Kimura Yoshinobu

  Department Of Agricultural Science Faculty Of Agriculture Okayama University

• Hirata K

  Laboratory Of Protein Chemistry And Engineering Graduate School Of Genetic Resources Technology Kyus

• Funatsu Gunki

  Laboratory Of Biochemistry And ** Laboratory Of Protein Chemistry & Engineering Faculty Of Agric

• HIRATA Koji

  Laboratory of Protein Chemistry and Engineering, Graduate School of Genetic Resources Technology, Ky

• Nakahara Yuko

  Laboratory Of Protein Chemistry And Engineering Faculty Of Agriculture Kyushu University

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