Abstract
6B3 antigen, a serum component released by various human malignant cells, was examined for its effect on cultured cells, and a possibility was raised that it suppresses B cell function. The 6B3 antigen, purified from culture supernatants of a human lung cancer cell line, HLC-2, can bind to the surface of surface immunoglobulin (sIg)-positive cells in general and exerts cytostatic and cytocidal effects on them. On the other hand, it did not bind to sIg-negative cells. The binding was inhibited by soluble immunoglobulins only at high concentrations, suggesting that the antigen, which has a decameric subunit structure, has strong affinity for clustered sIg, whereas its affinity for monomeric immunoglobulins is relatively low.
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