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  • Title: Kinetic evidence for activating and non-activating components of autophosphorylation of the insulin receptor protein kinase.
    Author: Kohanski RA, Lane MD.
    Journal: Biochem Biophys Res Commun; 1986 Feb 13; 134(3):1312-8. PubMed ID: 3004488.
    Abstract:
    Reduced and carboxamidomethylated-lysozyme (RCAM-lysozyme) is an excellent substrate (Km = 13 microM) and a potent inhibitor of receptor autophosphorylation (Ki = 0.6 microM). By using these properties of RCAM-lysozyme autophosphorylation was resolved into two kinetically and functionally distinct components involving formation of phosphotyrosine on the receptor's beta-subunits: 1. Insulin-stimulated autophosphorylation is independent of autophosphorylation at other sites; activation of insulin receptor-catalyzed substrate phosphorylation is dependent upon this component of autophosphorylation, which is inhibited by RCAM-lysozyme. 2. Autophosphorylation at saturating RCAM-lysozyme concentration is insensitive to insulin and has little effect on substrate phosphorylation. Thus, only insulin-dependent receptor autophosphorylation is responsible for activation of kinase-catalyzed substrate phosphorylation.
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