Heat-induced Aggregation between Ovalbumin and Lysozyme(Food & Nutrition)
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概要
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The heat-induced aggregation between ovalbumin and lysozyme was investigated under various conditions by measuring the development of turbidity. The result of sodium dodecylsulfate-polyacrylamide gel electrophoresis in the presence of 2-mercaptoethanol indicated that the obtained aggregate consisted of nearly the same amounts of ovalbumin and lysozyme. The heat-induced aggregation was inhibited by an increase of ionic strength. The effect of chemical modifications (succinylation and carboxymethylation) of the proteins on the heat-induced aggregation was examined to estimate the participation of specific amino acid residues in the aggregation process, the result indicating that the lysine and cysteine residues in the proteins were directly involved. From these results, it is suggested that the heat-induced aggregation between ovalbumin and lysozyme is due to an electrostatic attraction and sulfhydryl-disulfide interchange between the heat-denatured protein molecules.
- 1986-06-23
著者
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KOBAYASHI Kunihiko
Department of Pediatrics, Hokkaido University Graduate School of Medicine
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MATSUDOMI Naotoshi
Department of Agricultural Chemistry, Yamaguchi University
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Kobayashi K
Mitsubishi-kasei Institute Of Life Sciences
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Matsudomi Naotoshi
Department Of Agricultural Chemistry Faculty Of Agriculture Yamaguchi University
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Kobayashi K
Yamaguchi Univ. Yamaguchi Jpn
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YAMAMURA Yoshirou
Department of Agricultural Chemistry, Yamaguchi University
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Matsudomi N
Department Of Biological Chemistry Faculty Of Agriculture Yamaguchi University
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Matsudomi N
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 Orthopaedics Tokai University School Of Medicine
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Kobayashi Kunihiko
Department Of Agricultural Chemistry Faculty Of Agriclture Yamaguchi University
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