Aggregation between Lysozyme and Heat-denatured Ovalbumin
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概要
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The aggregation between lysozyme and heat-denatured ovalbumin was investigated by measuring the development of turbidity. The obtained aggregates were found to consist of lysozyme and ovalbumin at the molar ratio of 1.5, from the result of electrophoretic analysis. The aggregation was inhibited by the addition of NaCl or the acylation of lysozyme. This result suggests that the lysine residues in lysozyme were directly involved in the aggregation process. It is suggested that the cysteine residues in ovalbumin did not participate in the aggregation with lysozyme. The degree of aggregation reached its maximum when the ovalbumin solution was heated to 75°C, and was suppressed by the association of ovalbumin molecules during heat denaturation. From these results, it was found that lysozyme interacted electrostatically with the monomeric molecule of fully unfolded ovalbumin during aggregation.
- 社団法人 日本農芸化学会の論文
著者
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Matsudomi Naotoshi
Department Of Agricultural Chemistry Faculty Of Agriculture Yamaguchi University
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Yamamura Yoshirou
Department Of Agricultural Chemistry Yamaguchi University
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Kobayashi Kunihiko
Department Of Agricultural Chemistry Faculty Of Agriclture Yamaguchi University
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