Phosphorylation--dephosphorylation of purified insulin receptor from human placenta. Effect of insulin.
作者： F. Machicao , T. Urumow , O.H. Wieland
DOI: 10.1016/0014-5793(82)81079-X
关键词: Insulin receptor substrate 、 Phosphorylation 、 IRS2 、 Insulin 、 Insulin receptor 、 Chemistry 、 Insulin-like growth factor 1 receptor 、 GRB10 、 Biochemistry 、 Dephosphorylation
摘要: Abstract The insulin receptor of human placenta even after extensive purification is phosphorylated in the presence [γ-32P]ATP and NaF, dephosphorylated again on incubation NaF-free medium. Insulin stimulates phosphate incorporation into Mr95 000 subunit probably by activation phosphorylation step. Our data suggest that contains both kinase phosphatase activities may control state receptor.
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