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Fig. 6. Properties of {epsilon}-PKC binding to isolated F-actin. (A) Summary of {epsilon}-PKC binding to F-actin in the absence and presence of 50 µM arachidonic acid (AA). The line with solid circles (in the presence of AA) represents a fit to: B/Bmax=[{epsilon}-PKC]/([{epsilon}-PKC] + EC50), with EC50=110 nM and Bmax=18 pmol (or 180 pmol/mg protein). The stoichiometry of binding was 18 pmols {epsilon}-PKC bound per 2 nmoles actin monomers or a 1/110 ratio. Open circles represent {epsilon}-PKC with F-actin in the absence of AA. (B) Summary of inhibition of {epsilon}-PKC binding to F-actin by synthetic peptides. Data is represented as mean±s.e.m. from five experiments.