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Gel filtration studies were conducted with sugarcane leaf-protein preparations bearing strong phosphatase activity. The objectives were to isolate phosphatases from contaminant protein, and from one another. Sephadex, a dextran gel possessing variable sieving properties, was employed in 1.5 X 25-cm. columns packed and eluted with water or buffer. Good resolution of enzyme and protein constituents was obtained. Collecting 1-ml. fractions during a typical filtration, major phosphatase activitydoi:10.46429/jaupr.v50i4.3468 fatcat:3fmd62panffldnby5uhvmyq724