Differentiation of parotid and pancreatic amylase in human serum
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Amylase isolated chromatographically from normal human serum yields a polymorphic pattern of saccharogenic activity when subjected to disc electrophoresis on polyacrylamide gel. Parotid gland and salivary amylase exhibits an electrophoretic mobility similar to the more anodal peak observed in normal serum. The slower moving electrophoretic fraction of saccharogenic activity in normal serum appears to correspond to amylase derived from pancreatic tissue or that contained in duodenal aspirate. Differentiation of starch-hydrolyzing enzymes of various tissue origins in serum by means of disc electrophoresis may serve to enhance the clinical significance of the amylase determination.
KeywordsEnzyme Polyacrylamide Amylase Human Serum Electrophoretic Mobility
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