Taketo A, Taketo Y
Z Naturforsch C J Biosci. 1986 Mar;41(3):258-62. doi: 10.1515/znc-1986-0303.
When washed streptococci were incubated in a phosphate buffer containing MgSO4 and maltose (Bernheimer's basal medium) and centrifuged, no hemolytic activity was detected in the supernatant. Although incubation of the spent medium with carrier oligonucleotide did not yield active hemolysin, the mixture turned to be significantly hemolytic, upon ethanol precipitation and dehydration. Oxygen stability, sensitivity to trypan blue, absence in the spent medium from strain C203U, as well as chromatographic properties demonstrated that the hemolytic activity was due to streptolysin S-oligonucleotide complex. The latent streptolysin S was detected in the streptococcal culture supernatant as well. These results indicate that, even in the absence of exogenous carrier, streptolysin S is produced extracellularly by hemolytic streptococci but suffers rapid denaturation, and that the carrier oligonucleotide serves as an effector for the toxin peptide to assume active conformation, through noncovalent interaction. Effects of several protein denaturants were investigated on the toxin activation in vitro.
当洗涤后的链球菌在含有硫酸镁和麦芽糖的磷酸盐缓冲液（伯恩海默基础培养基）中孵育并离心后，在上清液中未检测到溶血活性。尽管用过的培养基与载体寡核苷酸孵育未产生活性溶血素，但经乙醇沉淀和脱水后，混合物变得具有显著的溶血活性。氧稳定性、对台盼蓝的敏感性、C203U菌株用过的培养基中不存在以及色谱特性表明，溶血活性归因于链球菌溶血素S - 寡核苷酸复合物。在链球菌培养上清液中也检测到了潜在的链球菌溶血素S。这些结果表明，即使在没有外源载体的情况下，溶血链球菌也能在细胞外产生链球菌溶血素S，但会迅速变性，并且载体寡核苷酸通过非共价相互作用作为毒素肽呈现活性构象的效应物。研究了几种蛋白质变性剂对体外毒素激活的影响。
