Tk polyagglutination produced in vitro by an endo-beta-galactosidase.
After treatment with the culture supernatant of Bacteroides fragilis or with an endo-beta-galactosidase from Escherichia freundii, the human red blood cells are Tk-activated, i.e. agglutinable by BS II lectin and their blood group I and i activities are reduced. These results suggest that B. fragilis produces an endo-beta-galactosidase activity and that the main antigenic determinant of Tk polyagglutinable red cells is a terminal N-acetyl-glucosamine residue.
D000371:Agglutination / Q000187:drug effects*; D001441:Bacteroides fragilis / Q000201:enzymology / Q000276:immunology; D004912:Erythrocytes / Q000187:drug effects / Q000276:immunology / Q000378:metabolism; D004925:Escherichia / Q000201:enzymology; D005696:Galactosidases / Q000494:pharmacology*; D006026:Glycoside Hydrolases; D001616:beta-Galactosidase / Q000378:metabolism / Q000494:pharmacology*
D005696:Galactosidases; D006026:Glycoside Hydrolases; C026093:keratan-sulfate endo-1,4-beta-galactosidase; D001616:beta-Galactosidase