Purification and Substrate Specificity of A Ginkgo biloba Glycosidase Active in β-1,2-Xylosidic Linkage in Plant Complex Type N-Glycans
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概要
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The β-xylosidase, which is active against plant complex type N-glycans, was purified to homogeneity from Ginkgo biloba seeds. The N-terminal amino acid sequence, G-S-A-A-G-N-R-, of the Ginkgo β-xylosidase (β-Xyl'ase Gb) was consistent with the deduced internal amino acid sequence of an Arabidopsis β-xylosidase (AtBXL1). β-Xyl'ase Gb hydrolyzed the β1-2 xylosyl residue from Xylβ1-2Manβ1-4GlcNAcβ1-4GlcNAc-PA and Xylβ1-2Manβ1-4GlcNAcβ1-4(Fucα1-3)GlcNAc-PA, but not that from Manα1-6(Manα1-3)(Xylβ1-2)Manβ1-4GlcNAcβ1-4(Fucα1-3)GlcNAc-PA.
著者
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Maeda Megumi
Department Of Biofunctional Chemistry Division Of Bioscience Graduate School Of Natural Science And
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Kimura Yoshinobu
Department Of Agricultural Science Faculty Of Agriculture Okayama University
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Akiyama Tsuyoshi
Department Of Applied Chemistry Faculty Of Engineering Kyushu University
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WOO Kwan
Department of Biofunctional Chemistry, Graduate School of Natural Science and Technology, Okayama University
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AKIYAMA Tsuyoshi
Department of Biofunctional Chemistry, Graduate School of Environmental and Life Science, Okayama University
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YOKOUCHI Daisuke
Department of Biofunctional Chemistry, Graduate School of Natural Science and Technology, Okayama University
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