Haemagglutinin of the antarctic seaweed Georgiella confluens (Reinsch) Kylin: isolation and partial characterization |
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Authors: | B W S Souza F K Andrade D I A Teixeira A Mansilla A L P Freitas |
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Institution: | 1. Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Fortaleza, Brazil 2. Unidade Acadêmica Especializada em Ciências Agrárias, Universidade Federal do Rio Grande do Norte, Natal, Brazil 3. Departamento de Ciencias y Recursos Naturales, Universidad de Magallanes, Punta Arenas, Chile 4. Instituto de Ecología y Biodiversidad, Santiago, Chile
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Abstract: | The marine red alga Georgiella confluens collected from Mackellar Inlet, King George Island, South Shetland Islands, Antarctic, was used in the isolation of a protein
with agglutinating activity. The Georgiella confluens haemagglutinin (GCH) was extracted with 20 mM phosphate buffer, pH 7.0, and purified through ion exchange chromatography,
followed by affinity chromatography on immobilized porcine stomach mucin. Among the erythrocytes analysed (human A, B and
O groups, rabbit and chicken), GCH agglutinated specifically chicken erythrocytes. Sodium dodecyl sulfate–polyacrylamide gel
electrophoresis of the haemagglutinin revealed a single band of 21.5 kDa, while by gel filtration on Sephadex G-100 its native
molecular mass was 25.5 kDa, suggesting that GCH is a monomeric protein. Haemagglutination studies showed that the GCH activity
was stable through temperature variations and did not exhibit divalent cation dependence. Furthermore, the haemagglutinin
was inhibited by the complex glycoproteins of porcine stomach mucin and fetuin, whereas the mono-, di-, and trisaccharides
tested showed no effect. |
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