The immunochemical properties of the macroamylases found in seven patients were examined. The class of heavy chain of the amylase-linked immunoglobulin was proved to be alpha in six cases and gamma in one case. The type of light chain was determined to be lambda in four cases, kappa in two cases, and kappa-lambda in one case. All the Ig A-amylase complexes were completely dissociated by Con-A affinity chromatography. The zymograms of dissociated amylase were normal. When free immunoglobulins released by acidification were mixed with purified human pancreatic or salivary amylase, the immunoglobulins recombined with both amylases in five cases, but only with pancreatic amylase and only with salivary amylase in one case, respectively. The precipitin line of Ig A-amylase complex, which was digested with papain, against anti-human Ig A/F (ab')
2 serum was proved to have amylase activity, but that against anti-human Ig A/Fc serum was proved not to have amylase activity. The result highly suggests that in Ig A-amylase complex amylase molecule links with Fab portion of Ig A molecule.
抄録全体を表示