Thakur I S
Department of Environmental Sciences, College of Basic Sciences and Humanities, G.B. Pant University of Agriculture and Technology, Pantnagar, Nainital, India.
Biochem Int. 1991 Feb;23(3):449-59.
Highly active glycoprotein allergens have been isolated from pollen of Prosopis juliflora by a combination of Sephadex G-100 gel filtration and Sodium dodecyl sulphate-Poly-acrylamide gel electrophoresis. The glycoprotein fraction was homogeneous, and had molecular weight 20,000. The purified glycoprotein allergen contained 20% carbohydrate, mainly arabinose and galactose. Enzymatic digestion of glycoprotein with protease released glycopeptides of molecular weight ranging from less than 1,000 to more than 5,000 on Sephadex G-25 gel filtration. Antigenicity or allergenicity testing of these glycopeptides by immunodiffusion, immunoelectrophoresis, and radioallergosorbent test indicated complete loss of allergenic activity after digestion with protease whereas incubation with beta-D-galactosidase and periodate oxidation had little affect on the allergenic activity of the glycoprotein fraction. But incubation with alpha-D-glucosidase did not affect the allergenic activity significantly. All these tests indicated that protein played significant role in allergenicity of P. juliflora pollen.
通过葡聚糖凝胶G - 100凝胶过滤和十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳相结合的方法，从牧豆树花粉中分离出了高活性糖蛋白过敏原。该糖蛋白组分是均一的，分子量为20,000。纯化的糖蛋白过敏原含有20%的碳水化合物，主要是阿拉伯糖和半乳糖。用蛋白酶对糖蛋白进行酶解后，在葡聚糖凝胶G - 25凝胶过滤中释放出分子量范围从小于1000到大于5000的糖肽。通过免疫扩散、免疫电泳和放射变应原吸附试验对这些糖肽进行抗原性或变应原性测试表明，用蛋白酶消化后变应原活性完全丧失，而用β - D - 半乳糖苷酶孵育和高碘酸盐氧化对糖蛋白组分的变应原活性影响很小。但是用α - D - 葡萄糖苷酶孵育对变应原活性没有显著影响。所有这些测试表明蛋白质在牧豆树花粉的变应原性中起重要作用。
