• 1 January 1979
    • journal article
    • research article
    • Vol. 30  (1) , 9-12
Abstract
An interaction of polyamines with protein kinases from T. cruzi epimastigotes was demonstrated. Spermine, spermidine and (less pronouncedly) putrescine inhibited protein kinase activities. In a T. cruzi extract 3 protein kinases were distinguished by their respective MW (> 200,000, 95,000 and 40,000) and preference for acceptor proteins (phosvitin and histones). The activity of the high MW protein kinase which phosphorylates phosvitin was strongly inhibited by spermine and spermidine. The type of inhibition by both polyamines was non-competitive with respect to ATP and phosvitin. The inhibition constants for spermine and spermidine were determined to be 1.4 mM and 2.0 mM, respectively.