盐法分离低核酸酵母蛋白的机理研究

STUDY ON THE MECHANISM OF SEPARATING YEAST PROTEIN WITH LOW NUCLEIC ACID CONTENT BY SALT TREATMENT

本文用荧光光谱法研究了不同盐对酵母蛋白质构象的影响,结果表明,盐是降低酵母蛋白分离物的核酸含量的原因之一。通过对盐除核酸过程进行热力学分折,对比离子对水结构和核蛋白稳定性的影响,否定了Damodaran提出的疏水作用机理,证明在维持核蛋白稳定的次级键中,氢键的作用是最主要的;核蛋白的解离并非盐通过改变溶剂的结构而间接作用于核蛋白所致,而应归因于盐与核蛋白的直接作用,特别是盐与核蛋白分子主链的作用。

In this paper the conformation change of yeast protein by different salts are studied by fluorescence spectrum with the result that salt is one of the reason why salt can reduce the nucleic acid content of isolated yeast protein (IYP). The process of removing nucleic acid by solt treatment is analyzed thermodynamically and the effects of ions on water structure are contrasted with that on stability of nucleoprotein. The results negated the hydrophobic mechanism by Damodaran and shows that hydrogen bond is the most important secondary bond stabilizing nucleoprotein, it is not the indirect action of salt on nucleoprotein through that changes the structure of solvent but the direct action of salt on nucleoprotein, especially the action of salt on the main chain of nucleoprotein molecules that causes nucleoprotein to dissociate.