title: Partial purification and characterization of the enterotoxin produced by Campylobacter jejuni.
abstract: 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.
authors.affiliation: Department of Food Science and Technology, Faculty of Fisheries, Hokkaido University, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Daikoku
authors.forename: M
authors.initials: M
authors.lastname: Kawaguchi
authors.forename: K
authors.initials: K
authors.lastname: Takama
authors.forename: S
authors.initials: S
authors.lastname: Suzuki
mesh_terms: D000262:Adenylyl Cyclases / Q000378:metabolism; D002168:Campylobacter fetus / Q000032:analysis*; D002772:Cholera Toxin / Q000276:immunology; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D004768:Enterotoxins / Q000302:isolation & purification* / Q000378:metabolism / Q000494:pharmacology; D006367:HeLa Cells; D000922:Immunotoxins / Q000276:immunology / Q000302:isolation & purification
chemical_list: D004768:Enterotoxins; D000922:Immunotoxins; D002772:Cholera Toxin; D000262:Adenylyl Cyclases