Membrane associated enzyme complexes containing lambda type immunoglobulin A

The properties of the membrane associated enzyme complexes were investigated. The enzyme complexes of alkaline phosphatase, arylamidase, and L-gamma-glutamyltranspeptidase were excluded by gel filtration on Sephadex G-200. The electrophoretic mobility of the enzyme complexes was found to be in the alpha-1 portion and these enzyme activities were immunologically fixed by anti-IgA and anti-light chain lambda antibodies. Heterogeneity in density was observed by density gradient ultracentrifugation. The activities of membrane-associated enzymes were demonstrated in both high (d > 1.21) and low density particles (1.063 < d < 1.21), and the enzyme activities of a high density particle were immunologically fixed by anti-IgA and anti-light chain lambda antibodies. The heterogeneity in density was based on the presence of immunoglobulin A molecule in the complexes. The specificity of the immunoglobulin which was found in the enzyme complexes proved to be exclusively of the alpha heavy chain classes and lambda light chain types respectively. This isotype specificity of immunoglobulin A is similar to the specificity observed in enzyme-linked immunoglobulins, and simple non-specific binding of immunoglobulin and membrane moiety was eliminated. This isotype specificity is of interest in connection with the properties of the circulating autoantibodies.