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Cells that were exposed to insulin or to Ca2+ show rapid changes in the phosphorylation of cellular proteins. These changes may be the consequence of the activation of a membrane-bound protein kinase which is induced by insulin treatment or may be due to the activation of a Ca2+-dependent kinase(s) linked with the insulin receptor. In the present paper, phosphorylation of different proteins by membrane-bound kinase(s) has been studied. By using affinity chromatography on immobilized insulin receptor, [32P]phosphate was found to be specifically incorporated in proteins which contained phosphotyrosine and phosphoserine. These proteins were isolated using anti-phosphotyrosine and anti-phosphoserine antibodies, respectively. Analysis of the phosphoproteins indicated that the activity of the membrane-bound kinase(s) in intact cells was not influenced by insulin, dibutyryl cAMP, or
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