Yasueda H, Mita H, Yui Y, Shida T
Int Arch Allergy Appl Immunol. 1986;81(3):214-23. doi: 10.1159/000234137.
Two purified allergens, designated as DF1 and DF2, were isolated from the extract of the whole culture of Dermatophagoides farinae by a combination of ammonium sulfate precipitation and ion exchange, hydrophobic, chelate and gel chromatography. DF1 was isolated as a heat-sensitive acidic protein with an apparent molecular weight of 25,000 and an isoelectric point of 4.6-7.2. DF2 was isolated as a heat-stable basic protein with an apparent molecular weight of 15,000 and an isoelectric point of 7.8-8.3. No allergenic cross-reactivity was seen between DF1 and DF2. Both DF1 and DF2 were shown to be the major allergens of D. farinae by the results of radioallergosorbent test and histamine release assay.
通过硫酸铵沉淀法与离子交换、疏水、螯合及凝胶色谱法相结合，从粉尘螨全培养物提取物中分离出两种纯化的变应原，分别命名为DF1和DF2。DF1被分离为一种热敏性酸性蛋白，表观分子量为25,000，等电点为4.6 - 7.2。DF2被分离为一种热稳定性碱性蛋白，表观分子量为15,000，等电点为7.8 - 8.3。DF1和DF2之间未见变应原交叉反应性。放射变应原吸附试验和组胺释放试验结果表明，DF1和DF2均为粉尘螨的主要变应原。
