Phaseolin seed variability in common bean (Phaseolus vulgaris L.) by capillary gel electrophoresis

Phaseolin, the major seed storage protein of Phaseolus vulgaris from forty-four wild and cultivated accessions, was studied using sodium dodecyl sulphate-capillary gel electrophoresis (SDS-CGE). In total, eleven phaseolin profiles, revealing polypeptide subunit variation in the range from 45.6 kDa to 54.4 kDa, were recorded. The number of polypeptide subunits recorded in particular profiles varied from 3 to 6; in total, eight phaseolin subunits were distinguished in the examined material. Ferguson plot analysis was used to correct non-ideal behaviour of phaseolin polypeptide subunits in capillary gel electrophoresis in the presence of SDS. The obtained results are compared to electrophoretic data received by slab polyacrylamide gel electrophoresis. The SDS-CGE method appears to provide a powerful tool for disclosure of phaseolin subunit variability.