Abstract
Gravidin, a phospholipase inhibitor characterised previously from amniotic fluid, was partially sequenced at the N-terminal and found to be identical to secretory component of human IgA. Inhibition of antiphospholipase activity was observed after incubation of gravidin with monoclonal antibody to human secretory component. Secretory component isolated from human saliva and breast milk was found to inhibit arachidonic acid release from human lymphocytes. It was concluded that gravidin is secretory component of IgA.
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