2-DE gel analysis of the Vista and King leaf proteomes. Proteins (350 μg) extracted from S. splendens leaves were separated in the first dimension by isoelectric focusing (pH 3–10) and in the second dimension by SDS-PAGE (12.5% (w/v) acrylamide). Proteins were visualized by silver staining. The 33 spots that showed significant volume changes caused by heat stress are labeled for both cultivars. A, Left gel, control Vista proteome. Right gel, heat-treated Vista proteome. B, Left gel, control King proteome. Right gel, heat-treated King proteome.