2005 Volume 19 Pages 204-208
Adsorption properties of proteins on c-axis oriented mesoporous HAp aggregates were investigated by liquid chromatography using the mesoporous HAp aggregates as an adsorbent. Elution molarity ratios of acidic proteins on the mesoporous HAp aggregates between before and after heat-treatment at 600°C increased with increasing the molecular weight in the order of ferritin > fibrinogen > catalase > BSA, whereas the elution molarity ratios of basic proteins were considerably lower than those of acidic proteins. These results suggested that the acidic proteins could be penetrated into the pore of the mesoporous HAp aggregates after heat treatment and were selectively adsorbed on the mesoporous wall consisting of the a-surface of the HAp aggregate. On the other hand, the basic proteins could be adsorbed on the wide outer surface of the plate-like HAp aggregates. Therefore, the elution molarity ratios of basic proteins decreased with decreasing the specific surface area by the heat treatment, independent of the mesoporous structure.
