Abstract
Normal and pathologic immunoglobulins were studied by micro-starch gel immuno-electrophoresis. With the buffer system used (tris-citrate and borate-NaOH), most of the immunoglobulins did penetrate into the starch gel, although a small percentage of the myeloma globulins and macroglobulins remained at the origin or penetrated only partially. The method was useful in studying the electrophoretic heterogeneity of the [gamma] 2 MM globulins and the polymer heterogeneity of the [gamma]1A MM globulins. Normal [gamma]1A-globulin produced a drawn-out asymmetric arc, owing to its electrophoretic heterogeneity, but most [gamma] 1A MM globulins produced several continuous zones of precipitate. A few [gamma]1A MM globulins were characterized by possessing mainly one component that penetrated either far into the gel or remained near the origin, although sera with [gamma]1A MM globulins of intermediate penetrance were also observed. 20 out of 25 sera of patients with macroglobulinemia contained macroglobulins that penetrated for considerable distance into the gel. Bence Jones proteins of group A produced single zones of precipitate, whereas Bence Jones proteins of group B produced two zones of approximately the same range of penetrance into the gel. Moreover, starch gel immuno-electrophoresis was useful in demonstrating Bence Jones proteins in sera from myeloma patients.