Partridge J, Shannon L, Gumpf D
Biochim Biophys Acta. 1976 Dec 21;451(2):470-83. doi: 10.1016/0304-4165(76)90142-2.
A lectin was isolated from barley seen which bound the coat glycoprotein of barley stripe mosaic virus (Type strain) and precipitated the virus from solution. Purification of the barley lectin was achieved by fractionation with ammonium sulfate and successive column chromatography on DEAE cellulose and cellulose phosphate. The barley lectin was homogeneous as ascertained by polyacrylamide gel electrophoresis, isoelectric focusing, and from immunochemical tests. No isolectins were detected. The lectin has a molecular weight of 31 000 daltons and is not a glycoprotein. Each virion can accomodate between 200 to 300 molecules of lectin. Barley lectin was shown to be specific for D-glucosamine, D-galactosamine and D-mannosamine with little distinction among the epimeric configurations at carbons 2 and 4. Free amino groups of D-glucosamine and D-galactosamine were detected on the coat glycoprotein of Type strain barley stripe mosaic virus and these sugars appear to serve as receptors for the barley lectin.
从大麦中分离出一种凝集素，它能结合大麦条纹花叶病毒（标准株系）的外壳糖蛋白，并使病毒从溶液中沉淀出来。通过硫酸铵分级分离以及在DEAE纤维素和磷酸纤维素上连续进行柱色谱法，实现了大麦凝集素的纯化。通过聚丙烯酰胺凝胶电泳、等电聚焦和免疫化学测试确定，该大麦凝集素是纯一的。未检测到同工凝集素。该凝集素的分子量为31000道尔顿，不是糖蛋白。每个病毒粒子可容纳200至300个凝集素分子。已表明大麦凝集素对D-葡糖胺、D-半乳糖胺和D-甘露糖胺具有特异性，在碳2和碳4处的差向异构体构型之间几乎没有区别。在标准株系大麦条纹花叶病毒的外壳糖蛋白上检测到了D-葡糖胺和D-半乳糖胺的游离氨基，这些糖似乎充当了大麦凝集素的受体。
