title: Partial characterization of hemagglutinin activity of the marine sponge Anthosigmella varians.
abstract: The marine sponge Anthosigmella varians contains proteins that agglutinate human erythrocytes irrespective of their ABO group antigens. The hemagglutination reaction depends on divalent cations and is not inhibited by L-arabinose, D-xylose, L-rhamnose, D-galactose, D-glucose, L and D-fucose, N-acetyl-D-galac-tosamine, N-acetyl-D-glucosamine, methyl-alpha-D-mannopiranoside, D-cellobiose, lactose, maltose, melibiose nor raffinose (33 mM each). A partial purification of the hemagglutinins with 31-fold increase in SA and 80% recovery of activity was obtained after gel filtration and ion-exchange gradient elution chromatography. Hemadsorption experiments carried out with the semipurified fraction using glutaraldehyde-fixed human erythrocytes suggest that proteins with molecular weight of 90 and 34 kDa participate in this reaction.
authors.affiliation: Departamento de Análises Clínicas e Toxicológicas, Faculdade de Farmácia, Universidade Federal da Bahia, Salvador, Brasil.
authors.forename: A M
authors.initials: AM
authors.lastname: Atta
authors.forename: A P
authors.initials: AP
authors.lastname: Cunha
authors.forename: S
authors.initials: S
authors.lastname: Peixinho
mesh_terms: D000818:Animals; D001938:Brazil; D002852:Chromatography, Ion Exchange; D006382:Hemadsorption; D006388:Hemagglutinins / Q000032:analysis*; D008970:Molecular Weight; D011161:Porifera / Q000737:chemistry*; D012623:Seawater
chemical_list: D006388:Hemagglutinins