苍耳花粉过敏原的纯化与鉴定

Purification and characterization of allergens from Xanthium strumarium pollen.

作者信息

Jaggi K S, Gangal S V

机构信息

CSIR Centre for Biochemicals, G.T.B. Marg, Delhi University Campus, India.

出版信息

Mol Cell Biochem. 1987 Dec;78(2):177-89. doi: 10.1007/BF00229692.

DOI:10.1007/BF00229692

PMID:3441253

Abstract

The allergenic components present in whole pollen extract of Xanthium strumarium were isolated by sequential ammonium sulphate precipitation, DEAE Sephadex A50 chromatography and gel filtration. The techniques of RAST inhibition and skin test were utilized to check the allergenicity of fractionated proteins revealing the presence of Xan Ib and Xan VIa as the important allergenic components. Xan Ib was found to be devoid of carbohydrate and had a molecular weight of 103,000 daltons. Xan VIa was a glycoprotein of molecular weight 17,000 daltons. The carbohydrate moiety of Xan VIa was found to be associated with allergenicity. The characteristic pattern of whole pollen extract on CIE and TLIEF showed 36 and 21 protein bands, respectively. The use of FPLC in isolation of partially purified allergens from Xanthium is discussed.

摘要

通过连续硫酸铵沉淀、DEAE 葡聚糖 A50 柱层析和凝胶过滤，分离出了苍耳全花粉提取物中的致敏成分。采用放射变应原吸附试验抑制法和皮肤试验技术，对分级分离的蛋白质的致敏性进行检测，结果显示 Xan Ib 和 Xan VIa 是重要的致敏成分。发现 Xan Ib 不含碳水化合物，分子量为 103,000 道尔顿。Xan VIa 是一种分子量为 17,000 道尔顿的糖蛋白。发现 Xan VIa 的碳水化合物部分与致敏性有关。苍耳全花粉提取物在免疫电泳（CIE）和薄层等电聚焦（TLIEF）上的特征图谱分别显示有 36 条和 21 条蛋白带。本文还讨论了使用快速蛋白质液相色谱（FPLC）从苍耳中分离部分纯化过敏原的方法。