A receptor specific for lipoglycans from Acholeplasma axanthum and Acholeplasma granularum was isolated from sheep erythrocyte stroma by extraction with n-pentanol and permeation chromatography. The purified receptor appeared as one band on sodium dodecyl sulfate-polyacrylamide gels and stained with Coomassie blue, periodate-Schiff reagent, and Sudan black. It was distinct from the erythrocyte receptor for gram-negative lipopolysaccharides and the glycophorin receptor for certain species of Mycoplasma. Periodate oxidation and trypsin did not affect the receptor activity in intact erythrocytes, but the purified receptor was susceptible to proteolytic digestion. Specific receptors, sensitive to trypsin digestion, could be isolated from rabbit kidney and cultured rabbit epidermal cell membranes. These could be distinguished from the receptor from erythrocytes by their solubility in n-pentanol. The segment of the lipoglycan molecule which binds to these receptors was not lipoidal in nature and was distinct from the specific antigenic determinants of the lipoglycans.