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建立配体印迹分析技术初步研究了嗜麦芽假单胞菌(Pseudomonas maltophilia)人绒毛膜促性腺激素(HCG)结合蛋白分子特点。纯化细菌HCG结合蛋白未经还原处理行SDS-PAGE分离后,再电泳转移至硝酸纤维膜上,~(125)I-HCG能与膜上70kd蛋白质发生特异结合。样品经还原加热处理或存在过量未标记HCG时,该放射性激素结合峰消失。此外,作者还用免疫印迹分析证实抗体识别带与放射性激素结合峰位置一致。以上结果表明细菌HCG结合蛋白分子量为70kd,二硫键在HCG结合活性中起重要作用。
Establishment of Latent Assay Technique The molecular characteristics of human chorionic gonadotropin (HCG) binding protein of Pseudomonas maltophilia were preliminary studied. The purified bacterial HCG-binding protein was separated by SDS-PAGE without reduction treatment and then electrophoretically transferred to the nitrocellulose membrane. Specific binding of ~ (125) I-HCG to the 70 kd protein on the membrane was achieved. The radionuclide binding peak disappears when the sample is reduced and heat treated or excess unlabeled HCG is present. In addition, the authors also used immunoblot analysis to confirm that the antibody recognition band was in line with the binding site of the radioactive hormone. The above results show that the bacterial HCG binding protein molecular weight of 70kd, disulfide bond in HCG binding activity plays an important role.