Blackshear P J, Nemenoff R A, Avruch J
FEBS Lett. 1983 Jul 25;158(2):243-6. doi: 10.1016/0014-5793(83)80587-0.
Insulin in the presence of Mn2+ and [gamma 32P]ATP promoted the phosphorylation of two proteins of Mr 95 000 and Mr 210 000 in detergent extracts of rat liver microsomes. The Mr 210 000 protein was identified as a component od the insulin receptor by immunoprecipitation. It also bound [125I]insulin specifically, was phosphorylated largely on a tyrosine residue and could not be cleaved to smaller subunits under extreme reducing conditions. The Mr 210 000 protein appears to be a component of a sub-population of liver membrane insulin receptors in which insulin-binding and insulin-stimulated tyrosine kinase phosphorylation site(s) reside in a single polypeptide chain.
在存在锰离子（Mn2+）和[γ-32P]三磷酸腺苷（ATP）的情况下，胰岛素促进了大鼠肝微粒体去污剂提取物中两种分子量分别为95000和210000的蛋白质的磷酸化。通过免疫沉淀法鉴定出分子量为210000的蛋白质是胰岛素受体的一个组分。它还能特异性结合[125I]胰岛素，主要在酪氨酸残基上发生磷酸化，并且在极端还原条件下不能裂解为更小的亚基。分子量为210000的蛋白质似乎是肝细胞膜胰岛素受体亚群的一个组分，其中胰岛素结合位点和胰岛素刺激的酪氨酸激酶磷酸化位点位于单一多肽链中。
