The D-galactose-binding lectin of the octocoral Sinularia lochmodes: characterization and possible relationship to the symbiotic dinoflagellates
| Autor: | Hisao Kamiya, Taishi Yanohara, Ryuichi Sakai, Kazuhiko Koike, Koji Muramoto, Kanae Koike, Mitsuru Jimbo |
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| Rok vydání: | 2000 |
| Předmět: |
Monosaccharide Transport Proteins
Physiology Molecular Sequence Data Biology Biochemistry Chromatography Affinity chemistry.chemical_compound Cnidaria Affinity chromatography Lectins Animals Amino Acid Sequence Lactose Melibiose Symbiosis Molecular Biology Base Sequence Lectin Galactose Fast protein liquid chromatography Genes rRNA Hemagglutination Tests Electrophoresis Disc Agglutination (biology) Microscopy Electron chemistry Galactosamine biology.protein Dinoflagellida Electrophoresis Polyacrylamide Gel Rabbits Sequence Alignment |
| Zdroj: | Comparative biochemistry and physiology. Part B, Biochemistrymolecular biology. 125(2) |
| ISSN: | 1096-4959 |
| Popis: | A d -galactose binding lectin (SLL-2) was isolated from Sinularia lochmodes, an octocoral, by a combination of affinity chromatography on acid-treated agarose and FPLC on Superdex 200. SLL-2 agglutinated rabbit and horse erythrocytes while SLL-1, a minor component, reacted only with rabbit erythrocytes. SLL-2 is a glycoprotein with a molecular mass of 122 kDa and is composed of eight identical subunits (15 kDa). The sequence of the amino terminal region of SLL-2 did not show any apparent homology to the sequences of other animal and plant lectins. d -Galactose, N-acetyl- d -galactosamine, lactose, and melibiose were moderate inhibitors to the agglutination of rabbit erythrocytes. In contrast, horse erythrocytes were much more susceptible to agglutination by SLL-2, which was inhibited by sugars and glycoproteins such as d -galactose, N-acetyl- d -galactosamine, lactose, melibiose, and porcine stomach mucin. SLL-2 showed considerable tolerance to heating and kept its activity after heating at 80°C for 60 min. In immuno-histochemical studies using an anti-SLL-2 antiserum and protein A gold conjugate, SLL-2 was found to be present in high amounts in the nematocysts. SLL-2 was also detected on the surface of symbiotic dinoflagellate, Symbiodinium sp. cells irrespective whether they were surrounded with or without host cells. These observations suggest the presence of lectin-mediated interaction between symbiotic dinoflagellates and S. lochmodes. |
| Databáze: | OpenAIRE |
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