Preliminary evidence that Clostridium perfringens type A enterotoxin is present in a 160,000-Mr complex in mammalian membranes.

摘要: Abstract Clostridium perfringens type A 125I-enterotoxin (125I-CPE) was bound to rabbit intestinal brush border membranes (BBMs) or Vero cells and then solubilized with 3-[(3-cholamidopropyl)dimethyl-ammonio]-1-propanesulfonate (CHAPS). Solubilized radioactivity analyzed by gel filtration chromatography on a Sepharose 4B column sodium dodecyl sulfate-polyacrylamide electrophoresis (SDS-PAGE) without sample boiling autoradiography. Specifically 125I-CPE extracted from either BBMs primarily associated complex of approximately 160,000 Mr. The CPE partially purified SDS-PAGE boiling. analysis the suggested that contains both 50,000-Mr protein 70,000-Mr in equimolar amounts. This result is supported affinity immobilized 4B, which showed specific interaction similar size proteins CPE. simplest explanation for these results (Mr 35,000) interacts eucaryotic form membrane-dependent These suggest receptor target site(s) are cells. significance findings terms binding, insertion, biologic action discussed.