Lehrer S B, Karr R M, Salvaggio J E
Clin Allergy. 1981 Jul;11(4):357-66. doi: 10.1111/j.1365-2222.1981.tb01606.x.
Coffee workers with occupational allergic symptoms and positive skin tests to green coffee bean and factor dust antigens have elevated serum IgE antibodies (by radioallergosorbent test--RAST) to green coffee and castor bean allergens. These antibodies were used in a RAST inhibition assay to analyse coffee and castor allergens. Bean allergens were extracted by homogenization in PBS, centrifugation and concentration of supernates by ultrafiltration. Green coffee bean allergens, fractionated by gel filtration and Pevikon block electrophoresis, were shown to be very heterogeneous with a molecular weight range of 50 000 to 500 000 daltons. Castor allergens were more homogeneous with a molecular weight of 14 000 daltons and were partially purified by Pevikon block electrophoresis, gel filtration and isoelectrofocusing. Chemical analysis showed that protein was the major component in both allergen extracts. However, proteolytic enzymes could only partially destroy allergenic activity. Such isolation and characterization of these allergens should result in better methods of diagnosis and treatment of coffee workers with occupational allergic disease.
有职业性过敏症状且对生咖啡豆和咖啡豆加工粉尘抗原皮肤试验呈阳性的咖啡工人,其血清中针对生咖啡和蓖麻籽过敏原的IgE抗体(通过放射变应原吸附试验——RAST法)升高。这些抗体用于RAST抑制试验以分析咖啡和蓖麻过敏原。通过在磷酸盐缓冲盐水中匀浆、离心以及用超滤法浓缩上清液来提取豆类过敏原。经凝胶过滤和聚乙烯醇缩甲乙醛区带电泳分级分离的生咖啡豆过敏原显示出非常不均一,分子量范围为50000至500000道尔顿。蓖麻过敏原更为均一,分子量为14000道尔顿,并通过聚乙烯醇缩甲乙醛区带电泳、凝胶过滤和等电聚焦进行部分纯化。化学分析表明蛋白质是两种过敏原提取物中的主要成分。然而,蛋白水解酶只能部分破坏过敏活性。对这些过敏原的此类分离和特性鉴定应能产生更好的方法来诊断和治疗患有职业性过敏性疾病的咖啡工人。