首页> 美国卫生研究院文献>Proceedings of the National Academy of Sciences of the United States of America >Cleavage of C2 by C1̄s̄ into the antigenically distinct fragments C2a and C2b: Demonstration of binding of C2b to C4b
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Cleavage of C2 by C1̄s̄ into the antigenically distinct fragments C2a and C2b: Demonstration of binding of C2b to C4b

机译:C1̄s̄将C2裂解为抗原截然不同的片段C2a和C2b:证明C2b与C4b的结合

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摘要

The activation of complement component C2 by C1̄s̄ is a major reaction step leading to the assembly of two related macromolecular enzymes in the classical complement pathway C3 convertase and C5 convertase. The present studies clearly document the smaller fragment, C2b, that results when human C2 reacts with C1̄s̄. We have identified and characterized C2b (34,000 daltons) as a single protein on disc electrophoresis and immunoelectrophoresis. C2a (73,000 daltons), the larger fragment from this reaction, has a more acidic nature and C2b is more basic. These fragments can also be detected by their different antigenic determinants. When the C2-C4b complex is activated in the fluid phase by C1̄s̄ and allowed to decay, it dissociates into C2a and the C2b-C4b complex. Furthermore, when C2 is bound to C4b-Sepharose and then reacted with C1̄s̄, only the C2a fragment is released from the solid phase C2-C4b-Sepharose into the fluid phase, and the C2b fragment remains noncovalently bound to C4b-Sepharose. These results suggest that the C2b portion of C2 contains a stable binding site for C4b and, after the decay release of C2a from this C3 convertase, the C2b fragment remains bound. Thus, the decay release of C2a may represent a temperature-dependent dissociation from C2b.
机译:C 1 ̄ s ̄ 是主要的反应步骤,导致经典补体途径C3转化酶中的两个相关大分子酶和C5转化酶。本研究清楚地记录了较小的片段C2b,该片段是人C2与C 1 ̄ 反应时产生的 s ̄ 。我们已经在圆盘电泳和免疫电泳中鉴定并鉴定了C2b(34,000道尔顿)作为一种蛋白质。 C2a(73,000道尔顿)是该反应的较大片段,具有更酸性的性质,C2b更具碱性。这些片段也可以通过其不同的抗原决定簇来检测。当C2-C4b配合物在液相中被C 1 ̄ 激活时, math> s ̄ 并允许其衰减,它分解为C2a和C2b-C4b络合物。此外,当C2与C4b-Sepharose结合,然后与C 1 ̄ 反应时 s ̄ ,只有C2a片段从固相C2-C4b-中释放琼脂糖凝胶进入液相,C2b片段仍与C4b-Sepharose非共价结合。这些结果表明,C2的C2b部分含有与C4b稳定的结合位点,并且在从该C3转化酶中释放出C2a后,C2b片段仍保持结合状态。因此,C2a的衰减释放可能表示与C2b的温度相关解离。

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