Protein chemistry and immunohistological study of macroamylasemia.

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Amylase binding mechanism were studied using purified macroamylase; which was obtained from macroamylasemia complicated by esophageal cancer exhibited antinuclear factor positive traits in clinical course, and in combination with immunohistological studies.1) Macroamylase was the IgA, k binding-type. 2) Purified IgA-amylase complex was in virtual agreement with the IgA sedimentation constant at 6.3s. 3) The complex P/S ratio was nearly 1.0. 4) Optimum temperature and optimum pH did not vary from normal amylase values; temperature and pH stability were increased. 5) Tissues obtained at autopsy were stained by the peroxidase antiperoxidase and immunofluorescence methods; IgA and amylase were observed in splenic endothelial cells and phagocytes.From the above data it appears that macroamylase consists of IgA and amylase with an unique binding mechanism which dose not influence amylase activity, and the possibility of participation by an immunological role.