酶法改性对蛋白质结构性质的影响及与酶特异性的关系——实验研究

EFFECT OF ENZYMATIGAL MODIFICATION ON THE STRUCTURAL PROPERTIES OF PROPERTIES OF PROTEINS AND ITS RELATIONSHIP WITH ENZYME SPECIFICITY --EXPERIMENTAL STUDY

研了酶作用对改性蛋白质结构性质的影响。实验结果充分表明:改性蛋白质的平均分子量与其水解度成反比关系。等电溶解度随水解度的增加成对数函数规律增加,极性与平均分子量成反比关系,柔性与平均分子量成负指数函数关系。这些均与理论研究结果一致。同时,憎水性随水解度的增加而呈反比例关系减小,而且与平均分子量成正比关系。根据以上结果,作者认为:改性蛋白质的平均分子量,极性,柔性和憎水性与酶作用之间存在明显的定量关系,可用来作为描述改性蛋白质结构性质的指标。

This paper studied the effect of enzyme on the structural propert ies of EMP ( enzymatical modified proteins ) by experimental research. The results following have been obtained from the experiments. The AMW ( average molecular weight ) of the EMP is inversely proportio- nal to the DH ( degree of hydrolysis ). The isoelectric solubility of EMP is logarithmic function of DH. The polarity of EMP is inversely proporational to the AMW. The flexibility of EMP is a negative exponential function of AMW. These results resembled theoretical study. The hycfrophobicity of EMP is inversely proportional to the DH, and is proportional to the AMW. In conclusion, the AMW, polarity, flexibility and hydrophobicity of EMP is closely related to the enzymatical modification, and could be used as the structural parameters for EMP.