Ford S A, Baldo B A, Weiner J, Sutherland S
Kolling Institute of Medical Research, Royal North Shore Hospital of Sydney, St Leonards, NSW.
Clin Exp Allergy. 1991 Mar;21(2):167-71. doi: 10.1111/j.1365-2222.1991.tb00826.x.
Jack-jumper ant venom proteins were electrophoretically separated on SDS-polyacrylamide gels, transferred to nitrocellulose and probed with sera from subjects who had experienced an allergic reaction after being bitten by a jack-jumper ant. Ant venom components that bound IgE antibodies were detected by addition of 125I-anti-human IgE followed by autoradiography. Of the 17 polypeptides resolved by electrophoresis only three, of molecular weights approximately 14 kD, 12 kD and 10 kD, bound IgE antibodies from the panel of 50 sera examined. There was a marked similarity in the binding patterns by individual sera with almost all of the sera recognizing the 14kD and 12 kD components. IgE-binding profiles of separated ant venoms from ants collected in different regions of Australia appeared to be very similar if not identical. Identification of the ant allergens is a necessary prelude to the preparation of standardized venom sac extracts suitable for safe and effective diagnostic and therapeutic use.
杰克跳蚁毒液蛋白在SDS-聚丙烯酰胺凝胶上进行电泳分离，转移至硝酸纤维素膜上，并用曾被杰克跳蚁叮咬后出现过敏反应的受试者的血清进行检测。通过加入¹²⁵I-抗人IgE，随后进行放射自显影，检测与IgE抗体结合的蚁毒成分。在通过电泳分离出的17种多肽中，只有分子量约为14kD、12kD和10kD的三种多肽与所检测的50份血清中的IgE抗体结合。各个血清的结合模式存在显著相似性，几乎所有血清都能识别14kD和12kD的成分。从澳大利亚不同地区采集的蚂蚁分离出的蚁毒的IgE结合谱即使不完全相同也非常相似。鉴定蚁类过敏原是制备适合安全有效诊断和治疗用途的标准化毒囊提取物的必要前奏。
