Properties of Abnormal Amylascs in Human Sera

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The properties of abnormal amylases which had unusually fast electrophoretic mobilityat beta-globulin portion by Cellogel electrophoresis and showed markedly reduced electro-phoretical mobility to the cathodic side by digestion with neuraminidase were studied. Theseabnormal amylases were found in three patients; one was a patient with chronic pancreatitis, the second was a patient with adenocarcinoma of pancreas, and the third was a patient withadenocarcinoma of the lung. These abnormal amylases had a close affinity for ConcanavalinA Sepharose and these bounded amylases were effectively displaced by the washing of alpha-methyl-D-mannoside containing buffer. The affinity of the abnormal amylases for theinsoluble potato starch was different from the amylases of normal human origin. Apparentdissociation constants (Ks) of abnormal amylases for soluble starch were different from thenormal human amylases. These facts were of interest in the studying the tumor producingamylases in sera,
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