Conditions have been adapted for the binding of intact bacteria to glycosphingolipids in a thin-layer chromatogram. Bacteria labeled externally with 125I or metabolically with other isotopes are layered on the plate and after repeated washing the bound bacteria are detected by autoradiography. Using this technique several kinds of bacteria have been shown to adhere to the plate in a carbohydrate-specific way with practically no background binding. Among the advantages of the method is the possible detection of a minor receptor component of a complex mixture extracted from a target cell, facilitating the isolation of the receptor for structural studies. In addition, the multivalent solid-phase presentation of the receptor candidate should also reveal low-affinity binding sites, which may escape detection in traditional inhibition experiments with soluble oligosaccharides.