title: Purification of a cell-associated hemagglutinin from Shigella dysenteriae type 1.
abstract: A cell-associated hemagglutinin (HA) was isolated and purified from a clinical isolate of Shigella dysenteriae type 1 by affinity chromatography on a fetuin-agarose column. The purified hemagglutinin produced a single-stained protein band of around 66 kDa in sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). In an immunodiffusion test, HA-antisera produced a single precipitin band against the purified HA without exhibiting any reactivity towards lipopolysaccharide (LPS) of S. dysenteriae type 1 strain. Inhibition of the hemagglutination by the glycoproteins fetuin, asialofetuin and a sugar derivative N-acetyl-neuraminic acid but not by simple sugars, suggested the specific requirement of complex carbohydrate for binding. Electron micrographs of the purified HA revealed a morphology typical of globular protein.
authors.affiliation: Division of Biochemistry, National Institute of Cholera and Enteric Diseases, Calcutta, India. icmrnice@ren.nic.in
authors.forename: B
authors.initials: B
authors.lastname: Guhathakurta
authors.forename: D
authors.initials: D
authors.lastname: Sasmal
authors.forename: A N
authors.initials: AN
authors.lastname: Ghosh
authors.forename: C R
authors.initials: CR
authors.lastname: Pal
authors.forename: A
authors.initials: A
authors.lastname: Datta
mesh_terms: D002477:Cells / Q000737:chemistry; D002846:Chromatography, Affinity; D006388:Hemagglutinins / Q000302:isolation & purification* / Q000648:ultrastructure; D012762:Shigella dysenteriae / Q000737:chemistry* / Q000145:classification; D000509:alpha-Fetoproteins
chemical_list: D006388:Hemagglutinins; D000509:alpha-Fetoproteins