Figure 6

Analysis of industrial pilot scale purification of GRFT. Representation of the purity, by SDS –PAGE a, and TMV CP content, by western blot b, of GRFT during industrial pilot scale purification. Sample volumes loaded on the gel were normalized to the initial extraction volume. The initial extract (1) contains both GRFT and TMV CP as well as other plant protein contaminants. The extract was pH adjusted to pH4 (2)heated (3) and filter pressed(4). After which the extract was incubated overnight with MgCl₂ and bentonite and simultaneousely filter pressed and sterile filtered (5). Samples 6–7 are the GRFT final product At 1x volume, 2xvolume and 15 μg of protein. Included for comparison was 1.5 μg and 3.0 μg of GRFT purified by the previously published methodology O’Keefe et al., [4] (5). The table represents the densitometric measures of GRFT and TMV protein content in the extracts.