Ataka M, Asai M
Research Institute for Polymers and Textiles, Ibaraki, Japan.
Biophys J. 1990 Sep;58(3):807-11. doi: 10.1016/S0006-3495(90)82425-5.
Concentration changes in supersaturated solutions during the nucleation and growth of the orthorhombic form of hen egg-white lysozyme crystals have been observed for 121 d at 35 degrees C and pH 4.6, and with 3% NaCl. The effect of a variation in the initial protein concentration on the rate of approach to solubility in equilibrium is analyzed, by applying a model, originally developed for the understanding of protein self-assembly. It is shown that the observed kinetics can be explained fairly well by this model, whose basic assumptions are that (a) the nucleation is induced by aggregation of i0 molecules into particular geometry, and (b) the growth proceeds via attachment of a monomer. The i0 value for this process is four, which agrees with the number of molecules in a unit cell. Similarity and dissimilarity of the observed crystal growth to that of low molecular weight substances are discussed.
在35℃、pH 4.6且含有3%氯化钠的条件下,对蛋清溶菌酶晶体正交晶型成核和生长过程中过饱和溶液的浓度变化进行了121天的观察。通过应用一个最初为理解蛋白质自组装而开发的模型,分析了初始蛋白质浓度变化对达到平衡溶解度速率的影响。结果表明,该模型能够较好地解释所观察到的动力学,其基本假设为:(a)成核是由i0个分子聚集形成特定几何形状诱导的;(b)生长通过单体附着进行。此过程的i0值为4,这与一个晶胞中的分子数一致。讨论了所观察到的晶体生长与低分子量物质晶体生长的异同。