Abstract
Spherical particles of cattle bone-originated apatites (r-HAp) were prepared by a consecutive procedure as dissolution-precipitation, spray-drying, and heat-treatment processes. The r-HAp particles obtained had effective pore structures for liquid chromatographic separation of the five proteins such as bovine serum albumin, myoglobin from horse skeletal muscle, ribonuclease A from bovine pancreas, lysozyme from chicken egg white, and cytochrome c from horse heart. The adsorption surface functions of the particles for the liquid chromatography were designed by optimizing the spray-drying conditions using a two fluid-nozzle and heat-treatment temperatures. The column packed with the r-HAp particles gave high resolution and excellent durability for the five proteins-separation because of no change in the pore size distribution curves even after more than sample injection of 300 times.
