Suzuki J, Yoshihara E, Kinoshita H, Nagamine Y, Kobayashi S
Department of Bioorganic chemistry, College of Environmental Health Azabu University, Japan.
Kansenshogaku Zasshi. 1996 Mar;70(3):278-82. doi: 10.11150/kansenshogakuzasshi1970.70.278.
The hemolysin produced by group B streptococci (GBH) has an isoelectric point (pI) of 5.8 and it shows a hemolytic activity in the absence of 2-mercaptoethanol (2-ME). The hemolytic activities of GBH were compared to that of streptolysin O (SLO) and streptolysin S (SLS). These hemolysins differed with respect to the binding and release of hemoglobin (Hb). GBH was bound to phospholipids on the membranes of target erythrocytes, followed by the gentle release of K+ and slow Hb release without lag time. Incontrast SLO released Hb as rapidly as K+. GBH induced hemolysis was inhibited by the addition of 30 mM raffinose. These results indicate that the effective diameter of the pores formed by GBH was about 1.1 nm. GBH showed a lower hemolytic efficiency than SLO, reflecting the fact that these hemolysins destroy erythrocytes by a different mechanism. Intracellular K+ and Hb were released at a different rate in GBH treated cells, indicating that a colloid-osmotic process is involved in the lytic mechanism.
B组链球菌（GBH）产生的溶血素的等电点（pI）为5.8，且在没有2-巯基乙醇（2-ME）的情况下表现出溶血活性。将GBH的溶血活性与链球菌溶血素O（SLO）和链球菌溶血素S（SLS）的溶血活性进行了比较。这些溶血素在血红蛋白（Hb）的结合和释放方面存在差异。GBH与靶红细胞膜上的磷脂结合，随后缓慢释放K+并缓慢释放Hb，无延迟时间。相比之下，SLO释放Hb的速度与释放K+的速度一样快。添加30 mM棉子糖可抑制GBH诱导的溶血。这些结果表明，GBH形成的孔的有效直径约为1.1 nm。GBH的溶血效率低于SLO，这反映了这些溶血素通过不同机制破坏红细胞的事实。在GBH处理的细胞中，细胞内K+和Hb以不同的速率释放，表明溶解机制涉及胶体渗透过程。
