Campylobacter jejuni enterotoxin was partially purified from culture supernatant. The purified fraction after gel filtration indicated three bands at 68, 54, and 43 kilodaltons on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). This fraction enhanced the adenylate cyclase activity of HeLa cell membranes by 1.5-fold over that of the control. The study with anti-cholera toxin immunoglobulin G (IgG) and ganglioside affinity column chromatographies revealed that the eluent from the anti-cholera toxin IgG column chromatography exhibited a single band (68 kDa) on SDS-PAGE and native PAGE, whereas the eluent from ganglioside column chromatography exhibited two bands (68 and 54 kDa) on SDS-PAGE. These suggest that the 68-kDa polypeptide should have an immunological relationship with cholera toxin, and the 68- and 54-kDa polypeptides might be responsible for the recognition of ganglioside
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