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  • Title: Phosvitin phosphate content. Implications for protein kinase assay.
    Author: Ahmed K, Wilson MJ, Davis AT.
    Journal: Biochim Biophys Acta; 1975 Jan 23; 377(1):80-3. PubMed ID: 1168073.
    Abstract:
    The maximal rates of the protein kinase (ATP: protein phosphotransferase, EC 2.7.1.37) reaction studied with chicken egg yolk phosvitin as substrate are dependent on the level of dephosphorylation of phosvitin. 30 per cent dephospho-phosvitin gives the optimal initial rates. With varying levels of dephosphorylation, the apparent Km for the substrate also changes in a biphasic manner. If this factor is taken into account, and a suitable adjustment is made for the concentration of dephospho-phosvitin in the reaction it is possible to achieve maximal rates for the kinase reaction with phosvitin preparations of varying levels of dephosphorylation. Such a consideration is important for comparing the results of protein kinase studies using phosvitin as the substrate.
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