These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Purification and characterization of Clostridium perfringens iota toxin: dependence on two nonlinked proteins for biological activity.
    Author: Stiles BG, Wilkins TD.
    Journal: Infect Immun; 1986 Dec; 54(3):683-8. PubMed ID: 2877949.
    Abstract:
    Clostridium perfringens type E iota toxin, a dermonecrotic and lethal binary toxin, was purified to homogeneity. Each protein component of the toxin, iota a (ia) or iota b (ib), appeared as a single band by gradient or sodium dodecyl sulfate-polyacrylamide gel electrophoresis and yielded a single immunoprecipitin arc by crossed immunoelectrophoresis with homologous antiserum. Individually, ia (Mr 47,500) or ib (Mr 71,500) had little biological activity. However, when combined in equimolar amounts, there was a 64-fold increase in the guinea pig dermonecrotic titer. The biological activity of ia was heat stable (85 degrees C for 15 min), whereas ib was inactivated at 55 degrees C. Our results demonstrated that C. perfringens iota toxin required two different, nonlinked protein components for biological activity.
    [Abstract] [Full Text] [Related] [New Search]