Assay of phosphotyrosyl protein phosphatase using synthetic peptide 1142–1153 of the insulin receptor

Authors:
  • GSGraham J. Sale
    Graham J. Sale

Abstract
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 K m values were 5 μM. V m values (nmol phosphate removed/min per mg protein) were 0.62 (particulate) and 0.2 (soluble). This corresponds to 80% of total activity being membrane‐associated, indicating that membrane‐bound phosphatases are important receptor phosphatases. The phosphatase activities were distinct from acid and alkaline phosphatase. In conclusion peptide 1142–1153 provides a useful tool for the further study and characterization of phosphotyrosyl protein phosphatases.

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