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Crude human placental extract was chromatographed on concanavalin A-Sepharose. Using a single procedure, 20- to over 300-fold purification of six acid glycohydrolases was achieved, in most cases with a good yield. Improved yield of individual enzymes could be achieved by modifications of the method of elution. The capacity of concanavalin A-Sepharose to bind glycohydrolases from placenta was very large, and will provice a useful procedure for the large-scale purification of the human enzymes.
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