Reconstitution of Phaseolus vulgaris α-Amylase Inhibitor from Isolated Subunits
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概要
- 論文の詳細を見る
The reconstitution of Phaseolus vulgaris α-amylase inhibitor from its two kinds of subunits was studied. The inhibitor was reconstituted by quick dilution from its subunits denatured in 6M guanidine hydrochloride with a concomitant restoration of the inhibitory activity. Various environmental factors had a profound influence on the rate and extent of the reconstitution. Especially low protein concentration and high ionic strength were essential for a high yield of regained activity, and Zn^<2+> was also effective in promoting reconstitution. The maximum specific activity of reconstituted inhibitor was obtained at a 1 : 1 molar ratio of α-subunit : β-subunit. Under the optimal conditions obtained, the activity regain was about 60% of the activity of the native inhibitor. Further, this report advances the possibility that the glycan chains of each subunit may be important in proper folding and assembly of the subunit polypeptides.
- 社団法人日本農芸化学会の論文
- 1994-01-23
著者
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Yamaguchi Haruki
Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture
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Higaki Hirofumi
Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture
関連論文
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- Structural Characterization of an α-Amylase Inhibitor from a Wild Common Bean (Phaseolus vulgaris): Insight into the Common Structural Features of Leguminous α-Amylase Inhibitors
- 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
- Promotion of Polypeptide Folding by interactions with Asn-Glycans
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- Intersubunit Cross-linking Study of the Subunit Structure of an α-Amylase Inhibitor from Phaseolus vulgaris White Kidney Bean
- 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.