トリプシン共存におけるハイドロタルサイト様化合物へのリン酸イオン交換の挙動

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A Cl^--intercalated hydrotalcite-like compound (HTAL) is a promising material as a better phosphate adsorbent for further clinical use than the currently marketed aluminum hydroxide gels. In the preceding study, we found that Cl^- ions in the interlayer of HTAL can be exchanged with phosphate ions equivalently. In the present study, we have investigated the adsorption of porcine pancreas trypsin on HTAL and the influence of trypsin adsorption on the phosphate/Cl^- ion-exchange properties of HTAL. The isotherm for trypsin adsorption at 310 K and pH 8.4 showed the curve of BDDT V type and gave an adsorption capacity of 88.6 mg/g for trypsin. The zeta-potential analysis of HTAL suggested that the trypsin adsorption on HTAL at pH 8.4 was restrained by the electrostatic repulsion between HTAL surface and trypsin with positive charge. XRD and nitrogen adsorption studies showed that trypsin was adsorbed on the external surface of HTAL by occupying the area (ca. 22 nm^2) per trypsin molecule. The phosphate/Cl^- ion-exchange reaction with HTAL was not affected by the presence of trypsin ; the phosphate ion-exchange capacity reached 73.6 mg P/g from the solution containing 3200 mg trypsin/dm^3. On the other hand, the trypsin adsorption was significantly depressed by the loading of phosphate ions. The XRD analysis of the phosphate-loaded HTAL revealed that the layered structure of hydrotalcite holds after the phosphate ion-exchange, but shows a slight increase of the interlayer distance from 0.3 nm to 0.5 nm by the intercalation of phosphate ions.
社団法人日本薬学会の論文
1994-01-25

トリプシン共存におけるハイドロタルサイト様化合物へのリン酸イオン交換の挙動

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