Kurinenko B M, Kashkin A P, Kalacheva N V, Meringova L V, Nekhoroshkova Z M
Biokhimiia. 1985 Apr;50(4):581-8.
Preparations of pancreatic RNAase modified by dextrane derivatives were obtained in an azocombination reaction. The UV absorption spectra and amino acid analysis of the preparations revealed quantitative and qualitative differences in the sites of the enzyme binding to the polymeric matrix depending on modification conditions. The observed differences in the binding sites of modified RNAase may be related both to the differences in the primary structure or even in the secondary and ternary structure of the enzyme. The latter observation was confirmed in studies of the antigenic properties of modified preparations. The interrelationship of these preparations with antibodies raised against native RNAase and the comparison of the degree of their antigenicity suggest the influence of modification on the antigenic properties of the protein. The number of binding sites of the enzyme to the support can be determined, which would neutralize the antigen-stimulated effect of the support due to the screening of protein antigenic determinants.
通过偶氮结合反应获得了由葡聚糖衍生物修饰的胰腺核糖核酸酶制剂。这些制剂的紫外吸收光谱和氨基酸分析表明，根据修饰条件，酶与聚合物基质结合位点存在定量和定性差异。修饰核糖核酸酶结合位点的观察到的差异可能与酶的一级结构甚至二级和三级结构的差异有关。后一观察结果在修饰制剂的抗原特性研究中得到证实。这些制剂与针对天然核糖核酸酶产生的抗体之间的相互关系以及它们抗原性程度的比较表明修饰对蛋白质抗原特性有影响。可以确定酶与载体的结合位点数，这将由于蛋白质抗原决定簇的屏蔽而抵消载体的抗原刺激作用。
