抄録
Cattle bone-originated apatites (r-HAp) powders were prepared by a dissolution-precipitation and subsequent heat-treatments at 673~1073 K. Adsorption characteristics on the r-HAp powders were investigated for different proteins such as bovine serum albumin (BSA), myoglobin from horse skeletal muscle (MOG), ribonuclease A from bovine pancreas (RBN), lysozyme from chicken egg white (LSZ), and cytochrome c from horse heart (CTC). The adsorption for each of the proteins obeyed the Langmuir equation. The saturated amounts of LSZ, CTC, and RBN (basic proteins with isoelectric points (E0) > 7.0) adsorbed (ASB) were 2~10 times larger than those of BSA and MOG (acidic proteins with E0 < 7.0) adsorbed (ASA). As the heat-treatment temperature was elevated, the ASB and ASA gradually increased, and the ratios of ASB to ASA decreased, and heats of adsorption for basic proteins increased, whereas those for acidic proteins decreased. These characteristic changes can contribute to a design of liquid chromatographic column for adsorption-separation of the proteins.
