The Journal of biological chemistry, 264(1), 602-610 (1989-01-05)
We are interested in developing methods to rigorously characterize the intrinsic enzymatic activity of the insulin receptor. We have previously shown that the intact, kinase active form of the receptor can be separated from inactive forms isolated from human placenta.
The Journal of biological chemistry, 261(21), 10000-10005 (1986-07-25)
Three peptides were synthesized corresponding to potential autophosphorylation sites of the beta subunit of the human insulin receptor. These were peptide 1150 corresponding to amino acids 1142-1153 of the pro-receptor, peptide 960 corresponding to amino acids 952-961 of the proreceptor
Synthetic peptide 1142-1153 of the insulin receptor was phosphorylated on tyrosine by the insulin receptor and found to be a potent substrate for dephosphorylation by rat liver particulate and soluble phosphotyrosyl protein phosphatases. Apparent Km values were approximately 5 microM.
