COVALENT BINDING AND HEMOLYTIC-ACTIVITY OF COMPLEMENT PROTEINS
COVALENT BINDING AND HEMOLYTIC-ACTIVITY OF COMPLEMENT PROTEINS
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DOI：
10.1073/pnas.77.12.7194
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发表时间：
1980-01-01
期刊：
影响因子：
--
通讯作者：
LEVINE, RP
中科院分区：
文献类型：
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作者：
LAW, SK;LICHTENBERG, NA;LEVINE, RP
据报道，羟胺可使补体第三种成分 (C3) 失活。 C3 溶血和共价结合活性以相同的动力学下降，表明这两种活性之间存在直接相关性。表面上共价结合的 C3b 显然具有溶血活性。相对于羟胺，C3 的失活是一级的。还研究了[14C]甲胺对C3 的灭活作用。失活与 C3d 结构域中 C3 的标记定量对应。获得的数据支持以下假设：C3 内存在内部硫酯，其在激活 C3b 时变得高度反应，并且 C3b 通过将硫酯的酰基官能团转移到接受表面上的羟基来与接受表面结合。这种 C3 与接受表面反应的模型也适用于 C4，C4 与膜表面共价结合，并且能够被羟胺和甲胺灭活。 C5 不会因胺处理而失活。 [使用了来自人和豚鼠的补体成分。]。
The inactivation of the 3rd component of complement (C3) by hydroxylamine is reported. C3 hemolytic and covalent binding activities decline with identical kinetics, demonstrating a direct correlation between the 2 activities. Apparently covalent, surface-bound C3b is hemolytically active. The inactivation of C3 is 1st order with respect to hydroxylamine. C3 inactivation with [14C]methylamine was also studied. The inactivation corresponds quantitatively with the labeling of C3 in the C3d domain. The data obtained support the following hypothesis: there is an internal thioester within C3 which becomes highly reactive on activation to C3b, and C3b binds to receptive surfaces by transfer of the acyl function of the thioester to a hydroxyl group on the receptive surface. This proposed model for the reaction of C3 with receptive surfaces also applies to C4, which binds to membrane surfaces covalently and is able to be inactivated by hydroxylamine and methylamine. C5 is not inactivated by treatment with the amines. [Complement components from human and guinea pig were used.].