Abstract
Analytical (50 μg) reversed-phase high-performance liquid chromatography (RP-HPLC) of fractions from soy protein purifications has been scaled up to injections in the preparative (1–200 mg) range to obtain sufficient quantities of glycinin subunits for sodium dodecyl sulfate-polyacrylamide gel electrophoresis characterization. We describe here the glycinin separations obtained by using analytical, semi-preparative, and preparative columns with an analytical gradient HPLC system. Parameters such as injection volume, flow-rate, and detector sensitivity are noted. Our results suggest that analytical RP-HPLC separationis of proteins can be conveniently scaled up in most HPLC systems.
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