Enzymes dissociated from corn (hybrid B73 x Mo17) seedling cell walls by solutions of high ionic strength possess the capacity to degrade Avena caryopsis glucan. Inhibitor studies disclosed that both endo-and exoenzyme activities were involved and that the reaction sequence paraleled the autolytic solubilization of fi-D-glucan in isolated cel waOls.The salt-dissociated exoenzyme activity was strongly inhibited by HgC12 and to a lesser extent by parachloromercuribenzoate at a concentration of 100 micromolar. In the absence of these inhibitors, A vena caryopsis glucan was converted to monosaccharide, whereas in the presence of the mercurials, only endoenzyme activity was apparent and the glucan substrate was hydrolyzed yielding products with an average molecular size of 1. (1,2,9,10,14,15,17,22,25,26,35). In many cases these enzymes were inadequately characterized,