Böhmer F D, Kurtskhalia T V, Grosse R, Girshovich A S
Biomed Biochim Acta. 1983;42(5):471-7.
Binding of 125I-insulin to Ehrlich ascites carcinoma cells revealed the presence of high affinity binding sites characterized by a dissociation constant of 6.1 . 10(-9) M and a number of sites per cell of 2.6 . 10(3). These values are in line with respective data for other cell types reported in the literature. The receptor was identified by photoaffinity labeling of highly purified plasma membranes with 4-azido-benzoyl-125I-insulin as a probe. The only receptor protein detectable has a molecular mass of 120-122 kD. This finding is discussed in terms of metabolic and cell proliferation effects of insulin.
125I标记胰岛素与艾氏腹水癌细胞的结合显示存在高亲和力结合位点，其解离常数为6.1×10⁻⁹ M，每个细胞的结合位点数为2.6×10³个。这些数值与文献中报道的其他细胞类型的相应数据一致。通过用4-叠氮苯甲酰-125I标记胰岛素作为探针，对高度纯化的质膜进行光亲和标记来鉴定该受体。唯一可检测到的受体蛋白的分子量为120 - 122 kD。从胰岛素的代谢和细胞增殖效应方面对这一发现进行了讨论。
