Different hydrolases were found to be present in the crude extract of dry de-embryonated wheat grains, including acid phosphatase. When the crude extract was chromatographed on a Wheat-Germ Agglutinin-Sepharose affinity column, an aliquot of acid phosphatase bound to the column and could be eluted specifically by N-acetyl-D-glucosamine solution. Some properties of the WGA-binding acid phosphatase (pH optimum, heat stability, Triton X-100 sensitivity, inhibition by some ions, molecular weight and Km) were studied. WGA appeared to have a stabilizing effect on the enzyme, while it was ineffective on the Km.