Characterization and biological activities of lectin isolated from Pinellia ternata

In this paper, Pinellia ternata lectin (PTL) purified from 95% saturated ammonium sulfate precipitation by applying mannose-Sepharose 4B affinity column chromatography was first described. The mannoseSepharose 4B affinity adsorption gel has already been designed and prepared before the experiments according the combinative characterization between lectin and mannose. Mass spectrometry analysis result shows that PTL is a glycoprotein with the molecular weight of 12.165 kD. It was conclude that PTL had strong agglutination effects on mouse red blood cells, and the minimum reaction concentration was 25 μg/ml according the Hemagglutination. Results of automatic amino acid analysis indicated that PTL mainly contained 15 varieties of amino acids, of which the minimum content was cysteine and aspartate was the maximum. Cell experiment results suggested that PTL of low concentrations (0.004 mg/ml, 0.02 mg/ml and 0.1 mg/ml) promoted HeLa cell proliferation, but the effect weakened with the concentrations and treated-time increasing. However, the HeLa cells proliferation was intensively inhibited by higher PTL concentrations (0.5 mg/ml and 1 mg/ml), and the effect increased in a dose and time dependent manner.