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A simple electrophoretic technique using thin layer polyacrylamide gel provided a good resolution of serum amylase isozymes with separation of up to 9 isozyme fractions. A strong oxidizing agent, ammonium persulfate, which had been used in polyacrylamide gel formation system, was removed by prior electrophoresis from the separating gel before sample application to avoid possible degradation of amylase molecule into subunits.From the results of electrophoretic mobility studies of serum, pancreatic and salivary amylase isozymes, it was concluded that amylase isozymes in human serum were of pancreatic and salivary origin.In patients with acute pancreatitis, increased amylase activities were observed on those of pancreatic origin. On the contrary, in patients with pancreatectomy, these isozyme activities disappeared from serum. In patients with mumps, amylase activities of salivary origin, which were observed in patients with pancreatectomy, increased in serum.