A novel lectin from the sponge Haliclona cratera: isolation,characterization and biological activity |
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Authors: | Pajic Ivana Kljajic Zoran Dogovic Nikola Sladic Dusan Juranic Zorica Gasic Miroslav J |
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Institution: | Faculty of Chemistry, University of Belgrade, Studentski trg 16, P.O. Box 158, YU-11001, Belgrade, Yugoslavia. |
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Abstract: | A lectin from the Adriatic sponge Haliclona cratera was purified by ion-exchange and gel chromatography. The molecular mass of the lectin is approximately 29 kDa. Purified lectin is rich in hydrophobic and basic amino acids and has an isoelectric point at pH 8.6. H. cratera lectin is relatively heat- and pH-stable. It agglutinates native and trypsinized, papainized and neuraminidase-treated human A, B, O, AB and sheep erythrocytes, and the hemagglutinating activity is independent of Ca(2+), Mn(2+) and Mg(2+) ions; D-galactose and N-acetyl-D-galactosamine are found to be moderate inhibitors of the activity. H. cratera lectin displays cytotoxic effect on HeLa and FemX cells and weak mitogenic effect on human T-lymphocytes pretreated with phytohemagglutinin (PHA). |
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Keywords: | Sponge Lectin Purification Isolation Stability Cytotoxicity |
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