N-Glycans Protect Proteins from Protease Digestion through Their Binding Affinities for Aromatic Amino Acid Residues.
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概要
- 論文の詳細を見る
It was previously revealed [Yamaguchi, H., Nishiyama, T., and Uchida, M. (1999) J. Biochem. 126, 261-265] that N-glycans of both the high-mannose and complex types have binding affinity for aromatic amino acid residues. This study shows that free N-glycans protect proteins from protease digestion through their binding affinities for the aromatic amino acid residues exposed on protein molecules. Protease digestion of bovine pancreatic RNase A and bovine a-lactalbumin was depressed in solutions (1 mM or so) of free N-glycans of both the high-mannose and complex types. The increasing order of the protective effects of the N-glycans paralleled that of their affinities for aromatic amino acid residues; and the presence of aromatic amino acids practically abolished the protective effects of the N-glycans. The N-glycans also depressed the protease digestion of metallothionein, an aromatic amino acid-free protein, in agreement with the observation that the N-glycans also interact with the solvent-exposed aromatic amino acid residues of the proteases. Thus it seems probable that the N-glycans protect proteins from protease digestion by steric hindrance attributable to their binding affinity for the solvent-exposed aromatic amino acid residues of both substrate proteins and proteases.
- 社団法人 日本生化学会の論文
著者
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KIMURA Naoya
Department of Applied Biological Chemistry, College of Agriculture, Osaka Prefecture University
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Ochi Fumiko
Department Of Applied Biological Chemistry College Of Agriculture Osaka Prefecture University
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Jitsuhara Yuki
Department Of Applied Biological Chemistry College Of Agriculture Osaka Prefecture University
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Nishiyama Tomoko
Department Of Anesthesiology Jr Tokyo General Hospital
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Yamaguchi Haruki
Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture
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Uchida Makoto
Department Of Applied Biological Chemistry College Of Agriculture Osaka Prefecture Unviersity
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