Electrophoretic behavior of serum amylase.

There have been several indications (1, 2) that the amylase found in serum is derived from sources other than the pancreas or salivary glands. For this reason we wished to determine whether any indication of fractionation of serum amylase could be obtained by paper electrophoresis. Although several accounts of the fractionation of amylase in serum are found in the literature, some involving precipitation and some involving electrophoresis, these data sometimes do not agree with one another and in other cases are rather limited. Cattaneo and Bassani (3), using acetone fractionation at low temperature, found that amylase in human serum always accompanied the albumin fraction, in horse serum, the globulin fraction. Baker and Pellegrino (4) using paper electrophoresis with human serum found amylase principally in the slow portion of the y-globulin with only small amounts in the more mobile fractions. Data for four subjects were presented. In paper electrophoresis with mouse serum, Delcourt and Delcourt (5) found amylase principally (about 75 per cent) in the pland &globulin fractions. Kunkel and Eberhard,’ in a single run using powdered plastic Geon in zone electrophoresis with human serum, found amylase mainly in the albumin fraction and a small amount with the al-globulin but none with the y-globulin fraction. In this study, serum fractions obtained by paper electrophoresis were analyzed by a micromodification of the amylase method of Van Loon et al. (6). Experiments in which serum was mixed with human saliva or pancreatic juice suggest the presence of some serum amylase different from salivary or pancreatic amylase.