Abstract
Wheat germ agglutinin binds to the surface of human platelets and leads to their agglutination. Unlike other aggregating agents, the clumping ability of platelets by the lectin was markedly reduced upon removal of the cell surface sialic acid. This reduction in agglutination of neuraminidase-treated platelets was due to a lower capacity of the cells to bind the lectin. Since the terminal sialic acid has been implicated in the clearance of platelets from the circulation, wheat germ agglutinin may prove to be a useful tool to explore those clinical conditions in which platelet survival is shortened.
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