Oligomerization and phase separation in globular protein solutions
Oligomerization and phase separation in globular protein solutions
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DOI：
10.1016/s0301-4622(98)00208-7
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发表时间：
1998-12-14
影响因子：
3.8
通讯作者：
Benedek, GB
中科院分区：
文献类型：
--
作者：
Asherie, N;Pande, J;Benedek, GB
我们已经化学交联的球状蛋白，γ（IIIb）-晶状体蛋白，产生一个系统的定义明确的低聚物：单体，二聚体，三聚体和混合物的较高的n-聚体。凝胶电泳，尺寸排阻色谱，准弹性光散射光谱，和电喷雾电离质谱被用来表征所形成的低聚物。测量了各种低聚物的液-液相分离边界。我们发现，在一个给定的浓度的相分离温度强烈增加的低聚物的分子量。这种相行为是非常相似的γ（II）-晶状体蛋白，其中氧化诱导的低聚伴随着相分离温度的增加以前的研究结果。这些发现意味着，对于相分离，蛋白质的表面性质的详细变化是不太重要的，比纯粹的空间效应的寡聚化。(C)1998 Elsevier Science B. V.保留所有权利。
We have chemically crosslinked a globular protein, gamma(IIIb)-crystallin, to produce a system of well-defined oligomers: monomers, dimers, trimers and a mixture of higher n-mers. Gel electrophoresis, size exclusion chromatography, quasielastic light scattering spectroscopy, and electrospray ionization mass spectrometry were used to characterize the oligomers formed. The liquid-liquid phase separation boundaries of the various oligomers were measured. We find that at a given concentration the phase separation temperature strongly increases with the molecular weight of the oligomers. This phase behavior is very similar to previous findings for gamma(II)-crystallin, for which oxidation-induced oligomerization is accompanied by an increase in the phase separation temperature. These findings imply that for phase separation, the detailed changes of the surface properties of the proteins are less important than the purely steric effects of oligomerization. (C) 1998 Elsevier Science B.V. All rights reserved.