液体クロマトグラフィーによるリン酸八カルシウムのタンパク質吸着特性

概要

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Adsorption characteristics of proteins on Ca_8H_2(PO_4)_6・5H_2O (OCP) were investigated by liquid chromatography using a potassium phosphate buffer (KP) as an eluant. Proteins as sample molecules with different isoelectric point (pI) values were adsorbed on the OCP surface equilibrated with 0.01 mol・dm^<-3> KP, and were desorbed with increasing KP molarity. Basic proteins with pI>6.8 were eluted by a using KCl or MgCl_2 linear molarity gradient, whereas acidic proteins with pI<6.8 were not eluted even at 0.3 mol・dm^<-3> KCl or MgCl_2. Such a chromatographic behavior was similar to that of Ca_<10>(PO_4)_6(OH)_2(HAp). It is presumed that acidic and basic proteins were adsorbed on the Ca^<2+> ions (Ca site) with positive charge and the PO_4^<3-> ions (P site) with negative charge on the surface of OCP, respectively. The amount of Ca site on the OCP surface were considered to be more than that on the HAp surface from average elution molarities for acidic and basic proteins. As the crystal surface structure of OCP (h00) was similar to that of HAp (h00), acidic proteins were preferentially adsorbed on the (h00) of OCP crystal with a blade-shaped form.
社団法人日本セラミックス協会の論文
1999-06-01