PURIFICATION AND CHARACTERIZATION OF HEMAGGLUTININ OF CLOSTRIDIUM BOTULINUM TYPE C STRAIN STOCKHOLM
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概要
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Clostridium botulinum type C hemagglutinin (HA) was purified and characterized for clarifying the function of HA in botulinum intoxication. The purified HA showed a single band on disc electrophoresis and a single precipitin line on agar gel double diffusion test. The specific activity of the purified HA was 1.6×10^4 units/mg protein for rat erythrocytes. The molecular weight of HA was 230,000 by ultracentrifuge analysis. HA bound not only to erythrocytes but also to intestinal cells. The HA activity was inhibited by the addition of gangliosides (GM_3,GM_4,GD_<1a>, GD_<1b>, and GT_<1b>) and fetuin, and was not shown to erythrocytes treated previously by neuraminidase. These results suggest that HA binds to sialic acid on cell surface. In botulinum intoxication, HA may play as a carrier for the internalization of toxin through small intestine cell.
- 北海道大学の論文
- 1986-10-31
著者
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Suzuki Norihiko
Department Of Biochemistry Faculty Of Veterinary Medicine Hokkaido University
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SYUTO Bunei
Department of Biochemistry, Faculty of Veterinary Medicine, Hokkaido University
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KUBO Shuichiro
Department of Biochemistry, Faculty of Veterinary Medicine, Hokkaido University
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Syuto Bunei
Department Of Biochemistry Faculty Of Veterinary Medicine Hokkaido University
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Kubo Shuichiro
Department Of Biochemistry Faculty Of Veterinary Medicine Hokkaido University
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SUZUKI Norihiko
Department of Biochemistry, Faculty of Veterinary Medicine, Hokkaido University
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