Abstract

Staphylococcus aureus β-haemolysin is secreted essentially by virulent strains from animals. The purification of the β-haemolysin described here includes two steps: glass-beads chromatography and chromatofocusing. The purity of the fraction obtained was investigated by acrylamide electrophoresis and immunoblotting with a monoclonal antibody directed against α-haemolysin and monospecific serum anti-β-haemolysin. Results showed a single band in the final product. The haemolytic activity measured initially in the culture supernatant was recovered in the final purified fraction and the specific activity was increased about 38,500-fold. The method described could also be valid for the simultaneous purification of the α- and β-haemolysins from a strain that produces the two toxins.

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