title: Binding of pig small intestinal mucin glycopeptides to fimbriated enterotoxigenic Escherichia coli.
abstract: Fimbriated enterotoxigenic Escherichia coli were found to specifically bind mucin glycopeptides from pig small intestine. Bacteria with N-acetyl galactosamine-specific fimbriae (F41) were found to have two populations of binding sites for mucin glycopeptides. High affinity sites (5 X 10(2) per cell) with a dissociation constant of 1 X 10(-7) M. Bacteria with sialic acid specific fimbriae (K99) were estimated to possess 3 X 10(3) binding sites per cell with a dissociation constant of 6 X 10(-7) M.
authors.affiliation: University of Agricultural Sciences, Uppsala, Sweden.
authors.forename: M
authors.initials: M
authors.lastname: Lindahl
authors.forename: I
authors.initials: I
authors.lastname: Carlstedt
mesh_terms: D000116:Acetylgalactosamine / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D004926:Escherichia coli / Q000378:metabolism*; D010861:Fimbriae, Bacterial / Q000378:metabolism*; D007413:Intestinal Mucosa / Q000378:metabolism*; D007421:Intestine, Small / Q000378:metabolism*; D009077:Mucins / Q000378:metabolism*; D019158:N-Acetylneuraminic Acid; D012794:Sialic Acids / Q000378:metabolism; D013045:Species Specificity; D013552:Swine
chemical_list: D009077:Mucins; D012794:Sialic Acids; D019158:N-Acetylneuraminic Acid; D000116:Acetylgalactosamine