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伴刀豆球蛋白A对溶血抗体功能活性的影响。

Effect of concanavalin A on the functional activity of hemolytic antibody.

作者信息

Langone J J, Boyle M D, Borsos T

出版信息

Immunol Commun. 1977;6(3):283-96. doi: 10.3109/08820137709050798.

Abstract

Concanavalin A (Con A), either in solution or insolubilized by covalent binding to Sepharose 4B, can inhibit the ability of fluid phase 19S, but not 7S, anti-Forssman antibody to sensitize sheep red cells (E) toward lysis by excess guinea pig complement. The efficiency of 19S antibody is unaffected when E are treated with Con A before sensitization or when antibody sensitized cells (EA) are exposed to the lectin before complement is added. Although whole complement activity is retained on a solumn of Con A-Sepharose, cell bound lectin did not act as a complement fixing antibody. Consistent with this result, there was no difference in the amount of C1 fixed by E and E-Con A, or by EA and EA-Con A.

摘要

伴刀豆球蛋白A(Con A),无论是处于溶液状态还是通过与琼脂糖4B共价结合而不溶解,都能抑制液相19S而非7S抗福斯曼抗体使绵羊红细胞(E)对过量豚鼠补体溶解产生致敏的能力。当在致敏前用Con A处理E或者在加入补体前将抗体致敏细胞(EA)暴露于凝集素时,19S抗体的效率不受影响。尽管整个补体活性保留在Con A-琼脂糖柱上,但细胞结合的凝集素并不作为补体结合抗体起作用。与该结果一致,E和E-Con A或EA和EA-Con A固定的C1量没有差异。

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