Secretion of a Phytohemagglutinin-Binding Glycoprotein in Man

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Abstract
Phytohemagglutinin (PHA) is a glycoprotein purified from the red kidney bean, Phaseolus vulgaris, which binds to and agglutinates the erythrocytes of many species, including man (1). This reaction occurs without apparent blood group specificity. The finding that N-acetyl-d-galactosamine competitively inhibits agglutination by PHA suggests that, like the blood group isoagglutinins, PHA binds to a specific site on the cell surface (2). A PHA-binding material has recently been isolated and characterized (3, 4). There is also evidence that certain serum proteins react with PHA (5). This report describes the presence in saliva and ovarian cyst fluid of a glycoprotein which reacts with PHA. Saliva was collected from normal donors and heated at 100°C for 10 min to inactivate salivary enzymes. After centrifugation at 1500 × G for 10 min, the opalescent supernatant fluid was tested for PHA hemagglutination-inhibition activity in the system described in Table I. Saliva from 30 individuals demonstrated hemagglutination-inhibition activity in dilutions up to 1:4. Inhibitory activity was independent of ABO group or secretor status. Ovarian cyst fluid demonstrated hemagglutination-inhibition activity in dilutions up to 1:16.

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