Kabanov V A, Mustafaev M I, Blokhina V D, Agaf'eva V S
Mol Biol (Mosk). 1980;14(1):64-75.
Interaction of gamma-globulin with quaternized poly-4-vinylpyridine in water solutions at pH 7 has been studied. Formation of soluble stable cooperative complexes has been observed in a wide range of component ratios. Protein globules are distributed unevenly between adsorbing polycations. Soluble complexes are rod-like particles assembled from the globules which are stabilized by polycation chains. Complex formation in the system gamma-G + PE is similar to that in the system BSA + PE. Competitive interaction of serum protein fractions was studied at the interacting with polycation. It has been shown that selectivity at binding protein fractions is observed in both artificially prepared systems (BSA + gamma-G, beta1-G + gamma-G, BSA + gamma-G + beta1-G), and in serum and whole blood. In those ratios where uneven distribution of protein molecules is observed the soluble complexes protein-PE are formed by separate distribution of individual proteins at the matrix. Decrease of PE concentration in the systems results in the formation of a soluble complex of mixed composition. When an insoluble complex is formed in the system serum-PE selective sorbtion of beta 2-globulin fractions is observed. The reasons for the selective sorbtion of various protein fractions are described, structural models of the soluble complexes protein-PE are suggested.
研究了γ-球蛋白与季铵化聚4-乙烯基吡啶在pH 7的水溶液中的相互作用。在很宽的组分比例范围内都观察到了可溶性稳定协同配合物的形成。蛋白质球状体在吸附性聚阳离子之间分布不均匀。可溶性配合物是由球状体组装而成的棒状颗粒，由聚阳离子链稳定。γ-G + PE体系中的配合物形成与BSA + PE体系中的相似。研究了血清蛋白组分在与聚阳离子相互作用时的竞争相互作用。结果表明，在人工制备的体系（BSA + γ-G、β1-G + γ-G、BSA + γ-G + β1-G）以及血清和全血中都观察到了结合蛋白组分的选择性。在观察到蛋白质分子分布不均匀的比例下，蛋白质-PE可溶性配合物是由单个蛋白质在基质上的单独分布形成的。体系中PE浓度的降低导致形成混合组成的可溶性配合物。当在血清-PE体系中形成不溶性配合物时，观察到β2-球蛋白组分的选择性吸附。描述了各种蛋白质组分选择性吸附的原因，提出了蛋白质-PE可溶性配合物的结构模型。
