Rees-Jones R W, Hedo J A, Zick Y, Roth J
Biochem Biophys Res Commun. 1983 Oct 31;116(2):417-22. doi: 10.1016/0006-291x(83)90539-9.
The alpha and beta subunits of the insulin receptor, Mr = 135K and 95K, appear to be synthesized via a single polypeptide precursor of Mr = 190K. We have investigated whether insulin stimulates the phosphorylation of this proreceptor, as is the case with mature receptor. Rat liver endoplasmic reticulum membranes were solubilized in Triton X-100 and chromatographed sequentially on wheat-germ agglutinin-agarose and lentil lectin-agarose columns. Phosphorylation of the lentil eluate with [gamma 32P]ATP revealed an insulin-stimulated phosphoprotein of Mr = 192K, which was recognized by antireceptor antibody, compatible with the receptor precursor. This suggests that further processing of the Mr = 190K insulin receptor precursor is not necessary for insulin binding, kinase activation, and receptor phosphorylation.
胰岛素受体的α和β亚基，分子量分别为135K和95K，似乎是通过一个分子量为190K的单一多肽前体合成的。我们研究了胰岛素是否像对成熟受体那样刺激这种前受体的磷酸化。将大鼠肝脏内质网膜在Triton X - 100中溶解，并依次在麦胚凝集素 - 琼脂糖柱和扁豆凝集素 - 琼脂糖柱上进行层析。用[γ-32P]ATP对扁豆凝集素洗脱液进行磷酸化，显示出一种分子量为192K的胰岛素刺激的磷蛋白，它能被抗受体抗体识别，与受体前体相符。这表明，对于胰岛素结合、激酶激活和受体磷酸化而言，分子量为190K的胰岛素受体前体的进一步加工并非必需。
