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为了探讨凝集素在豆科植物与根瘤菌的识别过程中的作用，用ＤＥＡＥ－３２离子交换层析和ＳｅｐｈａｄｅｘＧ－１５０凝胶过滤分离、纯化格拉姆柱花草种子凝集素（ＳＧＬ），其分子量约为４５ｋＤ，由两个相同的亚基组成，等电点约ｐＨ５．８，它是一种糖蛋白，含糖量约为２．６％．ＳＧＬ的热稳定性强．ＳＧＬ的血凝活性能被甘露糖所抑制．ＳＧＬ对红细胞的凝集作用可能具有种属专一性；ＳＧＬ具有强的促有丝分裂作用；荧光标记实验显示：９株能与格拉姆柱花草植株结瘤的菌株有７株能与ＳＧＬ结合，６株不能与之结瘤的菌株，只有１株能与ＳＧＬ结合，这表明不同根瘤菌菌株对ＳＧＬ的结合能力，和它们在格拉姆柱花草上结瘤能力之间可能具有一定的生物学相关性．
In order to investigate the role of lectin in recognition of legumes and rhizobia, DEAE-32 ion exchange chromatography and Sephadex G-150 gel filtration were used to separate and purify SGL. The molecular weight of 45 kD, consists of two identical subunits with an isoelectric point of about pH 5.8, which is a glycoprotein with a sugar content of about 2.6%. SGL thermal stability. The hemagglutination activity of SGL can be inhibited by mannose. The agglutination of erythrocytes by SGL may be species-specific; SGL has strong mitogenic activity; fluorescent labeling experiments show that: Only one of the strains that could not be nodulated could bind to SGL, indicating that there may be some biological correlation between the binding capacity of different Rhizobia strains to SGL and their ability to nodulate on the gerbera flower.