INSULIN INTERACTIONS WITH ITS RECEPTORS - EXPERIMENTAL EVIDENCE FOR NEGATIVE COOPERATIVITY
INSULIN INTERACTIONS WITH ITS RECEPTORS - EXPERIMENTAL EVIDENCE FOR NEGATIVE COOPERATIVITY
复制标题
DOI：
10.1016/s0006-291x(73)80072-5
复制
发表时间：
1973-01-01
影响因子：
3.1
通讯作者：
LESNIAK, MA
中科院分区：
文献类型：
--
作者：
DEMEYTS, P;ROTH, J;LESNIAK, MA
报道了一种简单的方法来检测多肽激素与其膜受体结合中的协同相互作用。放射性碘标记的激素从受体的解离研究在两种条件下：第一，通过稀释的标记物-受体复合物足以防止解离的示踪剂的再结合;第二，通过稀释到相同的程度在一个介质中含有过量的未标记的激素。如果位点是独立的，则两种情况下的解离速率必须相同。如果未标记激素的存在增加了示踪剂的解离速率，则必须发生负协同相互作用。培养的淋巴细胞和肝细胞膜上的胰岛素受体显示负协同作用。生长激素受体位点缺乏这些相互作用。
A simple method is reported to detect cooperative interactions in the binding of polypeptide hormones to their membrane receptors. The dissociation of radioiodinated hormone from the receptor is studied under two conditions: first, by diluting the hormone-receptor complex sufficiently to prevent rebinding of the dissociated tracer; second, by dilution to the same extent in a medium containing an excess of unlabeled hormone. If the sites are independent, the dissociation rates must be the same in both cases. If the presence of unlabeled hormone increases the dissociation rate of the tracer, negatively cooperative interactions must occur. Insulin receptors on cultured lymphocytes and liver plasma membranes show negative cooperative interactions. Growth hormone receptor sites lack these interactions.