Fig. 7. CrPRF has a high apparent affinity for maize pollen G-actin. A representative experiment shows that CrPRF shifts the steady state C_c (see below) for actin assembly. Increasing concentrations of pollen G-actin were polymerized alone (squares) or in the presence of 1 µM CrPRF (circles), 1 µM ZmPRO5 (diamonds) or 1 µM HPRO1 (triangles). The x-axis intercepts of each regression line (C_c values) were 0.29 µM in the absence of profilin and 0.74 µM, 0.71 µM and 0.91 µM in the presence of CrPRF, ZmPRO5 and HPRO1, respectively. The calculated apparent K_d values were 0.35 µM for CrPRF1, 0.40 µM for ZmPRO5 and 0.18 µM for HPRO1. Abbreviation: A.U., arbitrary light-scattering units.

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