羟基磷灰石钙对白蛋白的吸附

K. Kandori, S. Sawai, Y. Yamamoto, H. Saito, T. Ishikawa
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引用次数: 56

摘要

本文研究了牛血清白蛋白(BSA)在Ca/P摩尔比为1.55 ~ 1.70的羟基磷灰石钙(HAP)和经硅酸盐和氟离子改性的羟基磷灰石钙(HAP)表面在pH 6.0和288 K条件下的吸附性能。BSA在HAP颗粒上的吸附等温线为Langmuir型,吸附后会在HAP上产生负电荷。具有较大Ca/P摩尔比的未改性HAP粒子往往产生较大的电正zeta电位,这反过来又由于其静电吸引力而产生较大的饱和吸附BSA (ns)。硅酸盐离子的表面改性增加了HAP表面的酸性,使HAP表面的电负性更强,从而产生更小的ns值。相反,氟离子改性后的表面比未改性的表面增加了2倍。这一事实可以通过在HAP表面形成高碱性的CaF2来解释。
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Adsorption of albumin on calcium hydroxylapatite

Adsorption of bovine serum albumin (BSA) on calcium hydroxylapatite (HAP) with different Ca/P molar ratios ranging from 1.55 to 1.70 and on HAP surface-modified by silicate and fluoride ions has been studied at pH 6.0 and 288 K. The adsorption isotherms of BSA on HAP particles are of the Langmuir type and adsorption of BSA generated a negative charge on HAP. Unmodified HAP particles which have a larger Ca/P molar ratio tended to yield a larger electrically positive zeta potential, which in turn gave a larger saturated amount of adsorbed BSA (ns) as a result of their electrostatic attractive force. The surface modification by silicate ions increased the surface acidity and made the HAP surface more electrically negative so as to yield smaller ns values. On the contrary, surface modification by fluoride ions increased ns two-fold over that on the unmodified surface. This fact could be explained by the formation of highly basic CaF2 on the HAP surface.

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author index subject index Contact angle kinetics of human albumin solutions at solid surfaces Polymerization in non-aqueous lyotropic liquid crystals: Influence of the unsaturation site Micelle dissociation kinetics study by dynamic surface tension of micellar solutions
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