SEDIMENTATION EQUILIBRIUM IN MACROMOLECULAR SOLUTIONS OF ARBITRARY CONCENTRATION .1. SELF-ASSOCIATING PROTEINS
SEDIMENTATION EQUILIBRIUM IN MACROMOLECULAR SOLUTIONS OF ARBITRARY CONCENTRATION .1. SELF-ASSOCIATING PROTEINS
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DOI：
10.1002/bip.360260405
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发表时间：
1987-04-01
期刊：
影响因子：
2.9
通讯作者：
MINTON, AP
中科院分区：
文献类型：
--
作者：
CHATELIER, RC;MINTON, AP
给出了描述自缔合大分子溶液在任意浓度下沉降平衡的关系式。这些关系是通过使用标度粒子理论来计算在给定的径向扰动下存在的每个物种的热力学活性而获得的。预计结果是有效的球形蛋白质的解决方案的条件下，使个别溶质分子之间的相互作用可以近似由硬粒子的潜力。 沉降平衡的解决方案中包含一个nonassociated溶质或溶质，根据几个不同的计划，自协会模拟使用派生的关系。这些模拟的结果中提出的表观重均分子量溶质浓度的依赖性。简单的经验关系，估计真正的重均分子量的表观重均分子量，而不参考任何颗粒自缔合计划。以这种方式估计的重均分子量在所有实验上可实现的溶质浓度（< 400 g/L）下在真实重均分子量的百分之几内。
Relations describing sedimentation equilibrium in solutions of self-associating macromolecules at arbitrary concentrations are presented. These relationships are obtained by using scaled-particle theory to calculate the thermodynamic activity of each species present at a given radial disturbance. The results are expected to be valid for solutions of globular proteins under conditions such that interactions between individual solute molecules may be approximated by a hard-particle potential. Sedimentation equilibria in solutions containing either a nonassociating solute or a solute that self-associates according to several different schemes are simulated using the derived relations. The results of these simulations are presented in terms of the dependence of apparent weight-average molecular weight upon solute concentrations. Simple empirical relations are presented for estimating the true weight-average molecular weight from the apparent weight-average molecular weight, without reference to any particulate self-association scheme. The weight-average molecular weight estimated in this fashion is within a few percent of the true weight-average molecular weight at all experimentally realizable solute concentrations (< 400 g/L).