Isolation of the α₂-Globulin Pattern on Starch Gel

Abstract

zone electrophoresis of serum proteins in starch gels was first described by Smithies¹, who employed a borate buffer system and silver electrodes. Poulik² described a discontinuous system using tris (tri-hydroxymethylamino-methane) and borate buffers for the separation of proteins. Two-dimensional electrophoresis on paper, and then on starch gel as used by Smithies and Poulik^3,4, revealed at least six molecular size-groups in the α₂-globulin group. A modification of this method is described, which utilizes the combination of haptoglobins with hæmoglobin to give a faintly coloured band as visual marker of the α₂-region and thus avoids staining. Commercially available starch is used as supporting medium, and provides a wide separation of the individual fractions.