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[Isolation of the theta-hemolysin of Cl. perfringens]

Voprosy Meditsinskoi Khimii
|January 1, 1981
PubMed

Insights

Clostridium perfringens theta-toxin was purified using multiple chromatography techniques. The resulting homogenous theta-hemolysin exhibited high biological activity but was unstable, with a molecular weight of 53,000 daltons.

Area of Science:

  • Microbiology
  • Biochemistry

Context:

  • Clostridium perfringens is an opportunistic pathogen known to produce various toxins.
  • Theta-toxin (also known as perfringolysin O) is a major virulence factor contributing to tissue damage.

Purpose:

  • To describe the purification process of theta-hemolysin from Clostridium perfringens strain BP6K 28.
  • To characterize the biological activity and molecular weight of the purified enzyme.

Summary:

  • Theta-hemolysin was purified through a multi-step process involving isoelectric precipitation, DEAE cellulose chromatography, gel filtration, DEAE-Sephadex A-50 rechromatography, and affinity chromatography.
  • The homogenous theta-hemolysin demonstrated significant biological activity, causing complete hemolysis of human erythrocytes at levels exceeding 100,000 theta E per mg protein.
  • The purified enzyme was found to be highly labile, with a determined molecular weight of 53,000 daltons.

Impact:

  • Provides a detailed method for obtaining homogenous theta-hemolysin, crucial for further structural and functional studies.
  • Highlights the high specific activity of theta-hemolysin, underscoring its potent hemolytic and cytotoxic potential.
  • Characterizes the lability and molecular weight of theta-hemolysin, offering essential data for understanding its stability and interactions.

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