Granum P E
Biochim Biophys Acta. 1982 Oct 20;708(1):6-11. doi: 10.1016/0167-4838(82)90196-0.
The biological activity of Clostridium perfringens enterotoxin can be tested more precisely and with a much higher sensitivity by using the inhibition of protein synthesis by Vero cells, rather than the guinea pig skin test. Tryptic peptides of the enterotoxin produced in the presence of different concentrations of sodium dodecyl sulfate (0-1%) have been tested for biological activity (Vero cells) and inhibitory effect on cell-free protein synthesis (rabbit reticulocyte lysate). A fraction of tryptic peptides, about 16,000 daltons, was able to inhibit the cell-free protein synthesis, while the native enterotoxin had no such effect. The 16 kDa fraction had, however, lost the ability to disrupt the Vero cells (normal biological activity). It is probable that the enterotoxin has the double function (A and B chain), known from several other toxins, confined in its single polypeptide chain.
通过使用Vero细胞蛋白质合成抑制试验，而非豚鼠皮肤试验，可更精确且更灵敏地检测产气荚膜梭菌肠毒素的生物活性。已对在不同浓度十二烷基硫酸钠（0-1%）存在下产生的肠毒素的胰蛋白酶肽段进行了生物活性（Vero细胞）及对无细胞蛋白质合成抑制作用（兔网织红细胞裂解物）的测试。约16,000道尔顿的一部分胰蛋白酶肽段能够抑制无细胞蛋白质合成，而天然肠毒素则无此作用。然而，16 kDa的肽段已失去破坏Vero细胞的能力（正常生物活性）。肠毒素很可能具有其他几种毒素所共有的双重功能（A链和B链），且局限于其单一多肽链中。
