Purification and characterization of Sophora flavescens lectin

文献类型： 外文期刊

第一作者： Deng, JL

作者： Deng, JL;Zeng, ZK;Yan, B;Huang, XQ

作者机构：

关键词： Sophora flavescens lectin;inhibitory activity of lectin;sequence structure of N-terminal peptide

期刊名称：ACTA BOTANICA SINICA （ 影响因子：0.599； ）

ISSN： 0577-7496

年卷期： 2000 年 42 卷 8 期

页码：

收录情况： SCI

摘要： A lectin with strong hemagglutination activity was isolated from roots of Sophora flavescens Ait. by extraction, fractionation with (NH4)(2)SO4, ion-exchange chromatography on DEAE-Sepharose and followed by gel filtration on Sephadex G-150 and HPLC assay. The purified lectin showed a single protein band on PAGE and SDS-PAGE. The molecular weight of S. flavescens lectin was 32 kD when SDS-PAGE and Sephadex G-100 was used. The lectin agglutinated rabbit red blood cells at 0.97 mu g/mL and showed no specific agglutination with any type of human erythrocytes. The hemagglutination activity could be inhibited by mannose and levulose and slightly by glucose and maltose. The SFL contained 2.89% neutral saccharide. It could inhibit apparently the growth of the mycelium of Gibberlla saubinetii (Mont.) Sacc., Piricularia oryzae Cav. and Fusarium vasinfectum Atk. at the dosage of 62 mu g It was determined by Edman that the sequence of the N-terminal thirty amino acids was: T/A/VDXLXFTFSDFDPNGEDLLFQGDAHVTSNN.

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