Abstract
A complex of cardiolipin antigen (cardiolipin, phosphatidylcholine, and cholesterol) was immobilized in a triacetyl cellulose membrane. The membrane-bound antigen retained the immunochemical reactivity to bind specifically a corresponding free antibody (Wassermann antibody). A drastic membrane potential shift was associated with the immunochemical reaction between the membrane-bound antigen and the free antibody. The immunochemically induced potential shift is considered to result from a change of charge at the membrane—solution interface.
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