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霍乱毒素亚基B与神经节苷脂结合后亚基A的构象变化。

Conformational changes in subunit A of cholera toxin following the binding of ganglioside to subunit B.

作者信息

van Heyningen S U

出版信息

Eur J Biochem. 1982 Feb;122(2):333-7. doi: 10.1111/j.1432-1033.1982.tb05885.x.

DOI:10.1111/j.1432-1033.1982.tb05885.x
PMID:7060580
Abstract
  1. Cholera toxin has been labelled with the fluorescent probe 4-chloro-7-nitrobenzofuran (Nbf-Cl) in both subunits, and the labelled subunits separated by gel-permeation. They retained their biological activities. 2. Addition of ganglioside GM1 (which binds to subunit B only) to either labelled subunit did not alter the fluorescence of the Nbf probe. 3. Whole toxin was reconstituted using labelled subunit A and unlabelled subunit B. Addition of ganglioside GM1 to the reconstituted toxin enhanced the fluorescence by about 90%, but did not change the wavelength. This enhancement reached a maximum when the ganglioside to toxin ratio was about 1 to 1. Ganglioside GD1b (which does not bind) did not affect the fluorescence. 4. These results suggest that the binding of ganglioside to subunit B alters the environment of the Nbf probe bound to subunit A, presumably by a conformational change.
摘要
  1. 霍乱毒素的两个亚基均已用荧光探针4-氯-7-硝基苯并呋喃(Nbf-Cl)进行标记,标记后的亚基通过凝胶渗透法分离。它们保留了生物活性。2. 向任一标记亚基中添加仅与亚基B结合的神经节苷脂GM1,不会改变Nbf探针的荧光。3. 使用标记的亚基A和未标记的亚基B重构完整毒素。向重构毒素中添加神经节苷脂GM1可使荧光增强约90%,但不改变波长。当神经节苷脂与毒素的比例约为1比1时,这种增强达到最大值。不结合的神经节苷脂GD1b不影响荧光。4. 这些结果表明,神经节苷脂与亚基B的结合可能通过构象变化改变了与亚基A结合的Nbf探针的环境。

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1
Conformational changes in subunit A of cholera toxin following the binding of ganglioside to subunit B.霍乱毒素亚基B与神经节苷脂结合后亚基A的构象变化。
Eur J Biochem. 1982 Feb;122(2):333-7. doi: 10.1111/j.1432-1033.1982.tb05885.x.
2
Characterization of the cholera toxin receptor on Balb/c 3T3 cells as a ganglioside similar to, or identical with, ganglioside GM1. No evidence for galactoproteins with receptor activity.将Balb/c 3T3细胞上的霍乱毒素受体鉴定为一种与神经节苷脂GM1相似或相同的神经节苷脂。没有证据表明存在具有受体活性的半乳糖蛋白。
Biochem J. 1982 Apr 15;204(1):209-19. doi: 10.1042/bj2040209.
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Effects of ganglioside GM1 on the thermotropic behavior of cholera toxin B subunit.神经节苷脂GM1对霍乱毒素B亚基热致行为的影响。
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Analysis of cholera toxin-ganglioside interactions by flow cytometry.通过流式细胞术分析霍乱毒素与神经节苷脂的相互作用。
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Tryptophan residues of cholera toxin and its A and B protomers. Intrinsic fluorescence and solute quenching upon interacting with the ganglioside GM1, oligo-GM1, or dansylated oligo-GM1.霍乱毒素及其A和B亚基的色氨酸残基。与神经节苷脂GM1、寡聚GM1或丹磺酰化寡聚GM1相互作用时的固有荧光和溶质猝灭。
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Thermal stability and intersubunit interactions of cholera toxin in solution and in association with its cell-surface receptor ganglioside GM1.霍乱毒素在溶液中以及与细胞表面受体神经节苷脂GM1结合时的热稳定性和亚基间相互作用。
Biochemistry. 1988 Mar 22;27(6):2046-52. doi: 10.1021/bi00406a035.
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Capping of cholera toxin-ganglioside GM1 complexes on mouse lymphocytes is accompanied by co-capping of alpha-actinin.霍乱毒素-神经节苷脂GM1复合物在小鼠淋巴细胞上的封帽伴随着α-辅肌动蛋白的共同封帽。
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Conformational changes in cholera toxin B subunit-ganglioside GM1 complexes are elicited by environmental pH and evoke changes in membrane structure.霍乱毒素B亚基-神经节苷脂GM1复合物的构象变化由环境pH值引发,并引起膜结构的变化。
Biochemistry. 1997 Jul 29;36(30):9169-78. doi: 10.1021/bi962996p.
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Role of membrane gangliosides in the binding and action of bacterial toxins.膜神经节苷脂在细菌毒素结合及作用中的作用。
J Membr Biol. 1982;69(2):85-97. doi: 10.1007/BF01872268.

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