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免疫球蛋白G中的反应性二硫键。不同物种血清蛋白中的一个独特特征。

Reactive disulfide bonds in immunoglobulin G. A unique feature in serum proteins of different species.

作者信息

Schauenstein E, Schauenstein K, Dachs F, Reiter M, Leitsberger A, Weblacher M, Maninger K, Horejsi H, Steinschifter W, Hirschmann C, Felsner P

机构信息

Institute of Biochemistry, University of Graz, Austria.

出版信息

Biochem Mol Biol Int. 1996 Oct;40(3):433-46. doi: 10.1080/15216549600201003.

Abstract

A reactive disulfide bond (SS)* was detected and characterized in IgG of humans, rats and mice by virtue of disulfide interchange with dithionitrobenzoate. (SS)* was found exclusively in human IgG1 and rat IgG2b. In human IgG1 (SS)* was identified as the upper one of the two interheavy bridges in the hinge, where it appears to take part in complement activation. The biological significance of (SS)* in IgG was underlined by the fact that no other serum proteins were found to exhibit a similar reactivity.

摘要

通过与二硫代硝基苯甲酸进行二硫键交换,在人、大鼠和小鼠的IgG中检测并表征了一种反应性二硫键(SS)*。(SS)*仅在人IgG1和大鼠IgG2b中发现。在人IgG1中,(SS)*被确定为铰链区两条重链间桥中的上方那条,它似乎参与补体激活。未发现其他血清蛋白表现出类似反应性,这一事实突显了IgG中(SS)*的生物学意义。

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