Purification was substantially performed according to the same procedures as described in the previous lectin (Yagi etal, 1985). The supernatant of A. barbadensis gel was obtained by centrifugation of the homogenate and dialyzed against distilled water. Then the dialysate was evaporated under reduced pressure below 35 °C to produce a colored material. The non-dialysate dissolved in 0.02 M ammonium bicarbonate, pH 7.8, and was applied for further purification by a series of column chromatography of DEAE Sephadex A-25, Sepharose 6B and Sephadex G-50. The adsorbed fraction on DEAE Sephadex A-25 was eluted with a linear gradient of 0.3 M sodium chloride to produce two glycoprotein fractions. An active fraction was isolated from one of the fractions by further chromatographies on Sepharose 6B and Sephadex G-50.
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