Comment on a semi-pilot-scale procedure for isolating and purifying soybean (Glycine max) lectin.
Comment on a semi-pilot-scale procedure for isolating and purifying soybean (Glycine max) lectin.
复制标题
对分离和纯化大豆 (Glycine max) 凝集素的半中试规模程序进行评论。
DOI：
10.1021/jf030572d
复制
发表时间：
2004
影响因子：
6.1
通讯作者：
I. Liener
中科院分区：
文献类型：
--
作者：
I. Liener
Sir: The recent paper by Fasina et al.(1), which describes the large-scale purification of the soybean lectin, served to remind me of my own experience involving the isolation of this interesting protein over 50 years ago (2). In our effort to elucidate the poor nutritive value of raw soybeans, we succeeded in isolating from soybeans a protein that was toxic when injected into rats and which had the ability to agglutinate red blood cells. At the time we referred to this protein as “soyin” because the term “lectin” had not yet been proposed for this class of proteins (3). To establish the significance of this protein as a component of the diet that was capable of inhibiting growth, it became necessary to isolate large quantities of this protein for incorporation in the diet fed to rats (4). Utilizing the techniques of protein purification available to us at the time (isoelectric precipitation and fractionation with ammonium sulfate and ethanol), we succeeded in isolating 3 g of “soyin” starting with 1500 g of soy flour, equivalent to 2 g/kg, a procedure which could be completed within 10 days. It was of interest to compare these results with those reported by Fasina et al.(1), who isolated 5.4 g of the lectin from 3480 g of soyflakes. This translates into 1.4 g/kg and required 3 weeks to complete. In terms of purity, it should be pointed out that, on the basis of electrophoretic measurements, the lectin (also referred to as soyin) content of the preparation used in this study (4) represented78% of its total protein content. If necessary, further purification of the soybean lectin could be achieved by using the technique of affinity chromatography as described by Fasina et al.(1).
