Naberezhnykh G A, Sidorin E V, Dmitrenok P S, Kim N Yu, Solov'eva T F
Pacific Institute of Bioorganic Chemistry, Far East Division of the Russian Academy of Sciences, Vladivostok, 690022, Russia.
Biochemistry (Mosc). 2002 Sep;67(9):1062-7. doi: 10.1023/a:1020542523500.
A high molecular weight immunoglobulin-binding protein localized on the surface of bacterial cells has been isolated from the protein fraction of the outer membrane of Yersinia pseudotuberculosis, and its properties are described. The immunoglobulin-binding protein is a trypsin-resistant and temperature-sensitive beta-structured protein. As shown by MALDI-TOF mass spectrometry, after heating at 100 degrees C the molecular weight of the protein constituted 37.5 kD. The native protein is capable of interacting with human and rabbit IgG but looses the ability to bind the immunoglobulins after the temperature denaturation. The immunoglobulin-binding protein binds to the Fc-fragments of the immunoglobulins and binding depends on the presence of calcium ions.
一种定位于细菌细胞表面的高分子量免疫球蛋白结合蛋白已从假结核耶尔森氏菌外膜的蛋白质组分中分离出来，并对其性质进行了描述。该免疫球蛋白结合蛋白是一种抗胰蛋白酶且对温度敏感的β结构蛋白。如基质辅助激光解吸电离飞行时间质谱（MALDI - TOF）所示，在100℃加热后，该蛋白的分子量为37.5 kD。天然蛋白能够与人及兔IgG相互作用，但在温度变性后丧失结合免疫球蛋白的能力。该免疫球蛋白结合蛋白与免疫球蛋白的Fc片段结合，且这种结合依赖于钙离子的存在。
