Starch Gel Electrophoresis in a Discontinuous System of Buffers

Abstract

THE recently developed starch gel electrophoresis has proved to have a resolving power superior to any other type of zone electrophoresis^1–4. I have applied this technique to the study of highly purified toxins³, but further work on the separated and eluted fractions of the toxin of Corynebacterium diphtheriae in tissue cultures and in animals indicated that the resolution of these proteins was not completely satisfactory in the buffer (0.03 M boric acid and 0.012 M sodium hydroxide) normally used in this type of zone electrophoresis. A more suitable system was found with a mixture of tris-(hydroxymethyl)-aminomethane-citrate (tris-citrate) used in conjunction with a boric acid buffer. Preliminary results obtained with toxins, enzymes and human sera are briefly reported here.