The adsorption of two model proteins, albumin and lysozyme, by boehmite or amorphous aluminium hydroxyphosphate adjuvants was studied. Electrostatic, attraction has a major role in adsorption. At physiological pH, boehmite, which has a point of zero charge above 7.35, extensively adsorbed albumin, which has an isoelectric point of 4.8, but was not effective in adsorbing lysozyme (isoelectric point, 11.0). Conversely, amorphous aluminium hydroxyphosphate (point of zero charge, 4.0) was effective in adsorbing lysozyme but adsorbed relatively little albumin. The results suggest that the selection of either boehmite or amorphous aluminium hydroxyphosphate as an adjuvant should be based in part on the isoelectric point of the antigen.