Isolation, purification and characterization of a lectin from Lenzites sp.
2000
Quizon, R.V.
A mitogenic lectin has been isolated from the mushroom, Lenzites sp. by protein extraction using 0.02M phosphate buffered saline containing 0.15M NaCl(PSB), pH7.4, ammonium sulfate fractionation, gel chromatography using Sephadex G-200 and affinity chromatography. The Lenzites sp. lectin was an incomplete type of lectin since it needs trypsination of human erythrocytes before agglutination occurs. Results showed that fetuin, aglycoprotein, inhibited the agglutination of the erythrocytes by the lectin. Affinity chromatography using fetuin agarose column was used also for the purification of the Lenzites sp. lectin. The bound lectin was eluted with 0.1M Tris-Cl buffer in 0.5M NaCl. Polyacrylamide gel electrophoresis of lectin isolated either by gel chromatography or by affinity chromatography under non-denaturing condition gave one band with the same Rf value (0.1). The lectin was active at pH 5 to 10 and at 20 deg C to 60 Deg C. SDS-PAGE [sodium dodecyl sulfate - polyacrylamide gel electrophoresis] analysis of the purified lectin showed that it is a monomer with an estimated molecular weight of 184kD. The lectin is a glycoprotein with 0.30% total sugar. HPLC [high presssure liquid chromatography] analysis revealed the presence of glucose, galactose and maltose. The lectin did not inhibit the growth of bacteria such as Eschericia coli, Pseudomonas aeruginosa, Staphylococcus aureus and Bacillus cereus. Proliferation of cell lines Sarcoma 180 and lung cancer cells (A549) were stimulated by the Lenzites sp. lectin
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