Ligatin, a lectin that recognizes phosphorylated sugars, has been demonstrated in mammalian tissues to bind specific hydrolases to cell surfaces. Ligatin exists as a filament that can be released from membranes still complexed with its bound hydrolases by treatment of membrane preparations with CaCl2 and/or pH 8.0. The ligatin‐hydrolase complexes subsequently can be dissociated with ethyleneglycol‐bis(β‐amino‐ethyl ether) N, N′‐tetraacetic acid, resulting in a concurrent depolymerization of the ligatin filament. From membrane preparations of cerebrum, this procedure solubilized ligatin and a membrane‐bound acetylcholinesterase (EC 126.96.36.199). Binding of the cosolubilized acetylcholinesterase to ligatin could be demonstrated in vitro by affinity chromatography using the immobilized lectin. Ligatin‐hydrolase complexes have been shown to be dissociated by specific phosphorylated sugars (mannose 6‐phosphate and glucose 1‐phosphate). These sugars were also effective in eluting bound brain acetylcholinesterase from ligatin affinity columns. Analysis of labeled glycitols produced by tritiated borohydride reduction confirmed the presence of phosphorylated sugars on the ligatin‐cosolubilized material from brain. Copyright © 1982 Alan R. Liss, Inc.