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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Mechanism of the alpha-complementation reaction of E. coli beta-galactosidase deduced from fluorescence correlation spectroscopy measurements.
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Mechanism of the alpha-complementation reaction of E. coli beta-galactosidase deduced from fluorescence correlation spectroscopy measurements.

机译：从荧光相关光谱测量中推导的大肠杆菌β-半乳糖苷酶的α-互补反应的机理。

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摘要

The kinetics of the alpha-complementation reaction of two protein fragments yielding active E. coli beta-galactosidase was measured using fluorescence correlation spectroscopy (FCS). The association reaction was extremely slow with an apparent association rate kapp of 207 M-1 s-1. This low association rate can be explained by a fast pre-equilibrium and slow subsequent steps involving at least two dimeric complexes. The subsequent formation of a tetrameric complex is probable and consistent with the experimental data. The complexes comprise two or four subunits, respectively, of the large fragment (EA)2 and in all cases only one small fragment, ED which has been labeled with Cy5. These kinetics have been compared to the association kinetics of ED to inactivated (EA)2. The kinetics were similar to the association with native (EA)2. The data support the observation that lyophilization of (EA)2 in a reducing environment which causes complete loss of enzymatic activity does not interfere with binding.
机译：使用荧光相关光谱法（FCS）测量了两个产生活性大肠杆菌β-半乳糖苷酶的蛋白质片段的α互补反应的动力学。缔合反应非常缓慢，表观缔合速率kapp为207 M-1 s-1。如此低的缔合速率可以通过涉及至少两个二聚体复合物的快速预平衡和缓慢的后续步骤来解释。随后形成四聚体复合物的可能性与实验数据一致。该复合物分别包含大片段（EA）2的两个或四个亚基，在所有情况下，仅包含一个小片段ED（已用Cy5标记）。已将这些动力学与ED与灭活的（EA）2的缔合动力学进行了比较。动力学类似于与天然（EA）2的缔合。数据支持以下观察：在还原性环境中导致完全丧失酶活性的（EA）2冻干不会干扰结合。

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