Ganguly S
Department of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, New York 10461.
Oncogene. 1988 Sep;3(3):341-4.
A polyclonal anti-human placental insulin receptor antibody has been developed, and its interaction with the receptor has been studied in vitro. This antibody enhances insulin binding to the receptor, both in the immunoprecipitate and also in in vitro binding assay. In the Scatchard analysis of the insulin-receptor interaction, in the presence of the antiserum, a marked increase in Bmax is observed, while Kd remains more or less unaffected. This antibody recognizes insulin receptor from all tissues of old world monkey but does not recognize new world monkey, rat or mouse receptor. Insulin receptor binds to this antibody very strongly on a immunoaffinity column and cannot be eluted by gentle means, but it retains insulin stimulated tyrosine kinase activity while immobilized to immunoaffinity column. This antibody also activates insulin receptor mediated histone phosphorylation in vitro. It has been proposed that this antireceptor antibody modulates receptor function by causing conformational perturbation in vitro.
已研制出一种多克隆抗人胎盘胰岛素受体抗体，并在体外研究了其与该受体的相互作用。在免疫沉淀物中以及体外结合试验中，这种抗体均能增强胰岛素与受体的结合。在对胰岛素 - 受体相互作用的Scatchard分析中，在抗血清存在的情况下，观察到最大结合容量（Bmax）显著增加，而解离常数（Kd）或多或少未受影响。该抗体可识别旧世界猴所有组织中的胰岛素受体，但不能识别新世界猴、大鼠或小鼠的受体。胰岛素受体在免疫亲和柱上与这种抗体紧密结合，无法通过温和方法洗脱，但在固定于免疫亲和柱时仍保留胰岛素刺激的酪氨酸激酶活性。这种抗体在体外也能激活胰岛素受体介导的组蛋白磷酸化。有人提出，这种抗受体抗体通过在体外引起构象扰动来调节受体功能。
