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  • Title: Rapid assay of binding of tumor-promoting phorbol esters to protein kinase C1.
    Author: Tanaka Y, Miyake R, Kikkawa U, Nishizuka Y.
    Journal: J Biochem; 1986 Jan; 99(1):257-61. PubMed ID: 3457006.
    Abstract:
    Protein kinase C is generally accepted to be a receptor protein of tumor-promoting phorbol esters. The binding of [3H]phorbol-12,13-dibutyrate to protein kinase C can be assayed by a rapid filtration procedure using a glass-fiber filter that has been treated with a cationic polymer, polyethylenimine. The phorbol ester specifically binds to the protein kinase only in the presence of phosphatidylserine and calcium. Non-specific binding is less than 10%, at most, of the total binding. The binding is linear with respect to the concentration of protein kinase C, is dependent on the concentrations of phorbol ester and phosphatidylserine in a saturative manner, and is inhibited by diacylglycerol (an endogenous activator of the protein kinase).
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