A simple purification method for enterotoxin F produced byStaphylococcus aureusand some properties of the toxin

✍ Scribed by S. Notermans; J. B. Dufrenne

• Publisher: Springer Netherlands
• Year: 1982
• Tongue: English
• Weight: 452 KB
• Volume: 48
• Category: Article
• ISSN: 0003-6072
• DOI: 10.1007/bf00448416

✦ Synopsis

Staphyloccoccus aureus enterotoxin F (SEF), which is associated with S. aureus strains isolated from toxic-shock-syndrome patients, was purified by successive chromatography on CM sephadex C-25 and gelfiltration on sephadex G-75. When tested by disc-polyacrylamide gel-electrophoresis the toxin migrated as a homogeneous protein. In SDS-polyacrylamide gel-electrophoresis three protein bands were observed. The main component had a mol wt of 23000 and the two minor components had a tool wt < 13 000. By iso-electric focussing a main protein band with an iso-electric point of 7.2 was obtained. The LDs0 for rabbits (3-3.5 kg) by subcutaneous and intravenous application of SEF was 6/~g and 180 #g, respectively. Antibodies to SEF prepared in a sheep did not react with other staphylococcal enterotoxins (A to E).