Chemical Modification of the Hemolytic Lectin CEL-III by Succinic Anhydride : Involvement of Amino Groups in the Oligomerization Process
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概要
- 論文の詳細を見る
CEL-III is a Ca^<2+>-dependent lectin from a marine invertebrate, Cucumaria echinata, which shows strong hemolytic activity toward human and rabbit erythrocytes. After binding to carbohydrate receptors, CEL-III oligomerizes in the erythrocyte membrane to form ion-permeable pores, leading to the colloid osmotic rupture of the cells. Since hemolysis was greatly increased in the alkaline pH, especially above pH 9,involvement of amino groups of CEL-III in its hemolytic activity was evaluated using chemical modification by succinic anhydride. After modification of 7 amino groups per protein molecule, the hemolytic activity of CEL-III was reduced to 23% of the native protein, but hemagglutinating and carbohydrate-binding activities were only slightly affected even after modification of 14 amino groups. A circular dichroism spectrum of modified CEL-III showed almost no change in the secondary structure from that of the native protein, indicating that the decrease of hemolytic activity was not caused by partial unfolding of the protein. Immunoblotting analysis of the erythrocyte membrane treated with modified CEL-III showed a decrease in the formation of CEL-III oligomer in the membrane in parallel with the decrease in hemolytic activity. These results suggest that amino groups of CEL-III are involved in its oligomerization in the cell membrane, and their modification leads to inactivation of the protein without much influence on the carbohydrate-binding activity.
- 社団法人日本農芸化学会の論文
- 1998-06-23
著者
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HATAKEYAMA Tomomitsu
Department of Applied Chemistry, Faculty of Engineering, Nagasaki University
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Hatakeyama T
Department Of Applied Chemistry Faculty Of Engineering Nagasaki University
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Hatakeyama Tomomitsu
Laboratory Of Biochemistry Faculty Of Agriculture Kyushu University:(present Address)dept. Of Applie
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YAMASAKI Nobuyuki
Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University
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Aoyagi H
Department Of Applied Chemistry Faculty Of Engineering Nagasaki University
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AOYAGI Haruhiko
Department of Applied Chemistry, Faculty of Engineering, Nagasaki University
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Tomomitsu Hatakeyama
Department Of Applied Chemistry Faculty Of Engineering Nagasaki University
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Kodama H
Department Of Chemistry Faculty Of Science And Engineering Saga University
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Kuwahara H
Department Of Chemistry Faculty Of Science And Engineering Saga University
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Kodama Hiroaki
東京理科大学 薬学部分子病態学
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KUWAHARA Hiromiki
Department of Applied Chemistry, Faculty of Engineering, Nagasaki University
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FUNADA Takako
Department of Applied Chemistry, Faculty of Engineering, Nagasaki University
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MATSUYAMA Yumiko
Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University
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FUKUYAMA Sachiko
Department of Applied Chemistry, Faculty of Engineering, Nagasaki University
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Matsuyama Yumiko
Laboratory Of Biochemistry Faculty Of Agriculture Kyushu University
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Yamasaki Nobuyuki
Laboratory Of Biochemistry Faculty Of Agriculture Graduate School Kyushu University
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Yamasaki Nobuyuki
Laboratory Of Biochemistry And Laboratory Of Protein Chemistry And Engineering Faculty Of Agricultur
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Hatakeyama Tomomitsu
Department Of Agricultural Chemistry Faculty Of Agriculture Kyushu University
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Aoyagi Haruhiko
Department Of Applied Chemistry Faculty Of Engineering Nagasaki University
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Aoyagi Haruhiko
Faculty Of Pharmaceutical Science:faculty Of Science:kyushu University
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Yamasaki N
Laboratory Of Biochemistry Faculty Of Agriculture Graduate School Kyushu University
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Funada Takako
Department Of Applied Chemistry Faculty Of Engineering Nagasaki University
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Yamasaki Nobuyuki
Laboratory Of Biochemistry Department Of Bioscience And Biotechnology Graduate School Faculty Of Agr
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Fukuyama Sachiko
Department Of Applied Chemistry Faculty Of Engineering Nagasaki University
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Yamasaki Nobuyuki
Laboratory Of Agricultural Process Engineering Faculty Of Agriculture Kyushu University
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