Structural and Functional Properties of Hen Egg-white Lysozyme Deamidated by Protein Engineering
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概要
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The structural and functional properties of lysozymes genetically deamidated at positions 103 (N103D) and 106 (N106D) were studied by a protein engineering technique. The wild-type and mutant lysozymes were expressed in Saccharomyces cerevisiae and purified from the cultivation medium in two steps by cation-exchange chromatography on CM-Toyopearl. The lytic activity of deamidated lysozymes was almost the same as that of wild lysozyme, although the optimal pH of activity was slightly shifted to lower pH by the deamidation. The Gibbs free energy changes of unfolding (ΔG) at 20℃ for N103D and N106D were almost the same as that of wild-type. On the other hand, the structural flexibility of lysozymes, estimated by protease digestion, was significantly increased by the deamidation. The surface functional properties of deamidated lysozymes were considerably enhanced, compared to those of wild-type lysozyme. These results suggest that structural flexibility is an important governing factor in surface functional properties of proteins, regardless of their structural stability.
- 社団法人日本農芸化学会の論文
- 1992-09-23
著者
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Muraki Yoshifumi
Department Of Biochemistry Faculty Of Agriculture Yamaguchi University
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Kumagai Izumi
Department Of Biochemistry And Engineering Graduate School Of Engineering Tohoku University
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Kumagai Izumi
Department Of Industrial Chemistry Faculty Of Engineering The University Of Tokyo
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Tanimoto Shota
Department Of Biochemistry Faculty Of Agriculture Yamaguchi University
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Kato Akio
Department Of Agricultural Chemistry Faculty Of Agriclture Yamaguchi University
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Kobayashi Kunihiko
Department Of Agricultural Chemistry Faculty Of Agriclture Yamaguchi University
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