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A phytohemagglutinin has been isolated in 80 to 90% purity from the mushroom Agaricus campestris. This protein had a sedimentation constant of 4.2 S and an electrophoretic mobility, at pH 8.6, remindful of the properties of a fast γ-globulin. It was a nonspecific agglutinin reacting with erythrocytes and leukocytes from a number of species. The hemagglutination reaction was independent of temperature from 0–80° and of pH from 4 to 10, but was ionic strength dependent. The hemagglutination reaction was not inhibited by sugars but was inhibited by a red cell ghost sonic suspension. Enzymatic and chemical treatments of the sonically disintegrated inhibitor indicated that part or all of the inhibitor was a protein or polypeptide.
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Sage et al. (1967) studied this question.
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