Topological and Functional Characterization of the N-Glycans of Soybean(Glycine max) Agglutinin^1
スポンサーリンク
概要
- 論文の詳細を見る
- Japanese Biochemical Societyの論文
- 1999-07-01
著者
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Shibata Keiichi
Department Of Applied Biological Chemistry College Of Agriculture Osaka Prefecture University
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Yamaguchi Haruki
Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture
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MASAOKA Hironori
Department of Applied Biological Chemistry, College of Agriculture, Osaka Prefecture University
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Masaoka Hironori
Department Of Applied Biological Chemistry College Of Agriculture Osaka Prefecture University
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- Complete Sequence, Subunit Structure, and Complexes with Pancreatic α-Amylase of an α-Amylase Inhibitor from Phaseolus vulgaris White Kidney Beans
- N-Glycans Protect Proteins from Protease Digestion through Their Binding Affinities for Aromatic Amino Acid Residues^1
- Binding Affinity of N-Glycans for Aromatic Amino Acid Residues: Implications for Novel Interactions between N-Glycans and Proteins
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- A Chaperone-Like Function of Intramolecular High-Mannose Chains in the Oxidative Refolding of Bovine Pancreatic RNase B^1
- Topological and Functional Characterization of the N-Glycans of Soybean(Glycine max) Agglutinin^1
- Isolation and Characterization of the Subunits of a Heat-labile α-Amylase Inhibitor from Phaseolus vulgaris White Kidney Bean
- Reconstitution of Phaseolus vulgaris α-Amylase Inhibitor from Isolated Subunits
- Complete Sequence, Subunit Structure, and Complexes with Pancreatic .ALPHA.-Amylase of an .ALPHA.-Amylase Inhibitor from Phaseolus vulgaris White Kidney Beans.
- Identification of Essential Amino Acid Residues of an .ALPHA.-Amylase Inhibitor from Phaseolus vulgaris White Kidney Beans.
- N-Glycans Protect Proteins from Protease Digestion through Their Binding Affinities for Aromatic Amino Acid Residues.