Fahlbusch B, Rudeschko O, Müller W D, Schlenvoigt G, Vettermann S, Jäger L
Department of Clinical Immunology, University of Jena, Germany.
Int Arch Allergy Immunol. 1995 Oct;108(2):119-26. doi: 10.1159/000237128.
The major allergen from apple extract was concentrated by anion exchange chromatography and further purified by reverse-phase HPLC. A distinct peak with a high degree of homogeneity was obtained. The isolated protein has a MW of 18 kD and specific IgE-binding capacity (immunoblotting, IgE-binding inhibition). N-terminal amino acid analyses of the allergen allowed 37 cleavages and showed 67.6% identity to Bet v 1, the major allergen of birch pollen. Enzyme immunoassay inhibition studies with serum of birch/apple-allergic patients showed that besides cross-reacting structures to Bet v 1, apple-specific IgE antibodies could exist. Monoclonal antibodies (mAbs) were raised against the 18-kD allergen from apple and characterized by means of immunoblotting and ELISA. Only three of the eight studied mAbs reacted with Bet v 1.
苹果提取物中的主要过敏原通过阴离子交换色谱法进行浓缩，并通过反相高效液相色谱法进一步纯化。获得了一个具有高度均一性的独特峰。分离出的蛋白质分子量为18 kD，具有特异性IgE结合能力（免疫印迹法、IgE结合抑制）。对该过敏原进行N端氨基酸分析，得到37个裂解片段，与桦树花粉主要过敏原Bet v 1的同源性为67.6%。对桦树/苹果过敏患者血清进行酶免疫测定抑制研究表明，除了与Bet v 1有交叉反应的结构外，可能还存在苹果特异性IgE抗体。制备了针对苹果18-kD过敏原的单克隆抗体（mAb），并通过免疫印迹法和酶联免疫吸附测定法对其进行表征。在研究的8种mAb中，只有3种与Bet v 1发生反应。
