Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russia.
Int J Biol Macromol. 2012 Jun 1;50(5):1341-5. doi: 10.1016/j.ijbiomac.2012.03.015. Epub 2012 Mar 29.
Chaperone-like activities of α-crystallin, αB-crystallin and proline were studied using a test system based on aggregation of UV-irradiated glycogen phosphorylase b (Phb) from rabbit skeletal muscle. The biphasic character of the dependence of the initial rate of aggregation (v(agg)) of UV-irradiated Phb on the concentration of α-crystallin or αB-crystallin is indicative of the existence of two types of chaperone-protein substrate complexes differing significantly in affinity between the components of the complex. The dependence of v(agg) on the proline concentration is sigmoid (Hill coefficient is equal to 1.6) suggesting that the positive cooperative interactions between the proline molecules bound on the surface of the protein particles occur. When studying the combined suppressive action of α-crystallin and proline on aggregation of UV-irradiated Phb, a slight antagonism between proline used at a fixed concentration (0.15M) and α-crystallin was observed. At higher concentration of proline (0.5M) each chaperone acts independent of one another.
使用基于兔骨骼肌 UV 照射糖原磷酸化酶 b（Phb）聚集的测试系统，研究了α-晶体蛋白、αB-晶体蛋白和脯氨酸的伴侣样活性。UV 照射的 Phb 初始聚集速率（v(agg)）与 α-晶体蛋白或 αB-晶体蛋白浓度的双相依赖性表明存在两种类型的伴侣-蛋白底物复合物，它们在复合物成分之间的亲和力上有很大的不同。v(agg)对脯氨酸浓度的依赖性呈 S 形（Hill 系数等于 1.6），表明结合在蛋白颗粒表面的脯氨酸分子之间存在正协同相互作用。在研究α-晶体蛋白和脯氨酸对 UV 照射的 Phb 聚集的联合抑制作用时，观察到在固定浓度（0.15M）下使用脯氨酸时，与α-晶体蛋白之间存在轻微的拮抗作用。在更高浓度的脯氨酸（0.5M）下，每种伴侣蛋白都独立发挥作用。
