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Horizontal thin-layer polyacrylamide gel electrophoresis proved to provide a good resolution of urine amylase isozymes, with up to eight bands. In order to determine the source of amylase isozymes in urine, comparative studies were made on the electrophoretic mobilities of amylase bands in urine, salivary gland and pancreas homogenates obtained under the same condition. The results suggested that the amylase isozymes contained in urine consisted of those originated in pancreas and salivery glands. Storage of urine at 4°C and -18°C for 6 months resulted in no change of the mobilities of urine amylase isozymes. From these results, it seemed to be reasonable to determine the origin of each amylase isozyme on the basis of the electrophoretic mobility. Heat treatment of urine and saliva at 56°C for 6 hours caused no or slight reduction in amylase activity. The amylase activity of pancreatic juice, however, was completely inactivated by heat treatment at 56°C for 60 minutes. The mobility of each amylase isozyme did not change by the heat treatment, while, the activity of the isozyme AmyU-1 (pancreatic origin) showed marked reduction. This behavior suggests a possible physicochemical difference between the pancreatic and salivary amylases.

Electrophoretic studies on human urine amylase isozymes by using a simple thin-layer polyacrylamide gel electrophoresis