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  • 1
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 21 (1983), S. 305-314 
    ISSN: 0730-2312
    Keywords: protein kinase ; Plasmodium berghei ; Plasmodium chabaudi ; malaria ; polyamine stimulation ; quercetin inhibition ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Plasmodium berghei-infected murine red cells possess protein kinase activity that is associated with the isolated parasites. Schizonts contain significantly higher levels of this protein kinase than the more immature forms, suggesting a relationship between this enzyme activity and parasite development. Partially purified protein kinase has a Km for ATP of ∼30 μM, whereas the Km for GTP is ∼300 μM and the substrate preference is phosvitin 〉 casein 〉 〉 histone 〉 protamine. The Mg2+ optimum is 10-20 mM, and the protein kinase activity is stimulated by the polyamines spermine and spermidine. The flavone, quercetin, inhibits the protein kinase activity in a competitive manner with' respect to ATP (Ki ∼3 μM), and P chabaudi also has a very similarly regulated protein kinase. Protein kinases from both species are very similar to the type I casein kinase.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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