通过独立进行的组成梯度沉降平衡和组成梯度静态光散射测量来表征NADH氧化酶和过氧化物氧化还原蛋白的平衡异质缔合。从两个实验获得的结果都通过一个模型定量解释,根据该模型,在这些实验条件下,NADH氧化酶的二聚体与过氧化物氧还蛋白的十聚体形成1:1平衡复合物。发现从两种测量中获得的两种蛋白质的异缔合的最佳拟合平衡常数在两种方法的每种估计的不确定性范围内都相同。讨论了每种方法的相对优点。
The equilibrium hetero-association of NADH oxidase and
peroxiredoxin was characterized by means of independently conducted measurements of composition-gradient sedimentation equilibrium and composition-gradient static light scattering. Results obtained from both experiments were quantitatively accounted for by a model according to which a dimer of NADH oxidase forms a 1:1 equilibrium complex with a decamer of
peroxiredoxin under the conditions of these experiments. The best-fit equilibrium constants for heteroassociation of the two proteins obtained from the two measurements were found to be identical to well within the uncertainty of estimate of each of the two methods. The relative virtues of each of the methods are discussed.