牛骨由来アパタイト粉末の調製と異種たんぱく質吸着特性によるキャラクタリゼーション

概要

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Cattle bone-originate apatite (r-HAp) prepared by a dissolution-precipitation method had a Ca^<2＋>-deficient structure containing small amounts of Mg^<2＋> and Na^＋ions. The r-Hap powder, which consisted of aggregates of microcrystals 20〜30 nm in size，was found to be more advantageous as an adsorbent than a hydroxyapatite powder synthehesized from reagents, because of its large specific surface area 100m^2 ･g^<-1>. For the r-Hap powder, the adsorption for each of the five different proteins ? bovine serum albumin (BSA)，myoglobine from horse skeletal muscle(MOG), ribonuclease A from bovine pancreas (RBN), lysozyme from chicken egg white (LSZ)，and cytochrome-c from horse heart (CTC)−obeyed the Langmuir equation. The saturated amounts of LSZ and CTC (isoelectric points (E-o)＜7.0) adsorbed were 2〜15 times larger than those of BSA and MOG (E-o＜7.0) adsorbed. The basic and acidic proteins can be selectively adsorbed on the P-and C-sites of the hydroxyapatite surface, repectively , suggesting that on the r-HAp surface，the number of P-sites would be greater than the number of C-sites.
北見工業大学の論文