Inhibition of protein synthesis by a tryptic polypeptide of Clostridium perfringens type A enterotoxin.
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.
D000818:Animals; D002460:Cell Line; D002474:Cell-Free System; D003016:Clostridium perfringens; D004768:Enterotoxins / Q000378:metabolism*; D000882:Haplorhini; D010446:Peptide Fragments / Q000494:pharmacology*; D014176:Protein Biosynthesis / Q000187:drug effects; D012967:Sodium Dodecyl Sulfate; D014357:Trypsin / Q000378:metabolism*
D004768:Enterotoxins; D010446:Peptide Fragments; D012967:Sodium Dodecyl Sulfate; D014357:Trypsin