Abstract
Of 20 kinds of plant lectins examined, agglutinin activity of only mushroom lectin was inhibited with non-hemoglobin proteins of the red cell lysate. Chromatography of non-hemoglobin proteins on DEAE-cellulose and on hydroxylapatite resulted in isolating a protein which gave a single precipitation line with esterase activity in immunoelectrophoresis. SDS-polyacrylamide gel disc electrophoresis demonstrated that the protein consisted of two subunits molecular weight of which was approximately 100,000 each.
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